Π‘ΡΡΡΠΊΡΡΡΠ½ΠΎ-ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΠ΅ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ²
Π 1979 Π³ΠΎΠ΄Ρ La Noue ΠΈ ΡΠΎΠ°Π²Ρ. (LaNoue and Schoolwerth, 1979) ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Π²Π²Π΅Π΄Π΅Π½ΠΈΡ ΡΠ°Π΄ΠΈΠ°ΠΊΡΠΈΠ²Π½ΠΎΠΉ ΠΌΠ΅ΡΠΊΠΈ Π² ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ, ΡΡΠ°Π½ΡΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΠΉ ΠΏΠ΅ΡΠ΅Π½ΠΎΡ ΠΊΠΎΡΠΎΡΡΡ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°Π»ΡΡ, Π±ΡΠ»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π½ΡΡΡΠ΅Π½Π½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ Π½Π΅ ΡΠ²Π»ΡΠ΅ΡΡΡ Π½Π΅ΠΏΡΠ΅ΠΎΠ΄ΠΎΠ»ΠΈΠΌΡΠΌ ΠΏΡΠ΅ΠΏΡΡΡΡΠ²ΠΈΠ΅ΠΌ Π΄Π»Ρ ΠΎΠ±ΠΌΠ΅Π½Π° ΠΌΠ΅ΠΆΠ΄Ρ ΡΠΈΡΠΎΠ·ΠΎΠ»Π΅ΠΌ ΠΈ ΠΌΠ°ΡΡΠΈΠΊΡΠΎΠΌ. Π§Π΅ΡΠ΅Π· 10 Π»Π΅Ρ ΡΡΠ°Π»ΠΎ ΠΈΠ·Π²Π΅ΡΡΠ½ΠΎ ΠΎ ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΎΠ΄ΠΈΠ½Π½Π°Π΄ΡΠ°ΡΠΈ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌ Π²ΠΎ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
- Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΡΠ΄Π΅ΡΠΆΠΊΠ°
- ΠΠΈΡΠ΅ΡΠ°ΡΡΡΠ°
- ΠΡΡΠ³ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ
- ΠΠΎΠΌΠΎΡΡ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ
Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- Π‘ΠΠΠ‘ΠΠ Π‘ΠΠΠ ΠΠ©ΠΠΠΠ
- ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«
- 1. ΠΠ΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π°
- 1. 1. ΠΠ΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π½Π°Ρ ΡΠ΅Π°ΠΊΡΠΈΡ ΠΈ Π΅Π΅ ΡΠΎΠ»Ρ Π² ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΌ ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΠ·ΠΌΠ΅
- 1. 2. ΠΠ·ΠΎΠ·ΠΈΠΌΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ ΡΠΊΠ°Π½Π΅ΠΉ ΠΌΠ»Π΅ΠΊΠΎΠΏΠΈΡΠ°ΡΡΠΈΡ
- 1. 3. ΠΠ½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½Π°Ρ Π»ΠΎΠΊΠ°Π»ΠΈΠ·Π°ΡΠΈΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ
- 1. 4. Π‘Π²ΡΠ·ΡΠ²Π°Π½ΠΈΠ΅ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ Ρ ΠΏΠΎΡΠΈΠ½ΠΎΠΌ
- 1. 5. ΠΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ ΠΈΠ·ΡΡΠ΅Π½ΠΈΡ Π°Π΄ΡΠΎΡΠ±ΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΠΎΠ²Π΅Π΄Π΅Π½ΠΈΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ
- 2. ΠΠΈΡΠΎΡ
ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΉ ΠΏΠΎΡΠΈΠ½
- 2. 1. ΠΠ΄Π΅Π½ΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΠΏΠΎΡΠΈΠ½Π° ΠΊΠ°ΠΊ Π±Π΅Π»ΠΊΠ° ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ°
- 2. 2. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅, ΠΎΡΠΈΡΡΠΊΠ° ΠΈ ΡΠΎΡΡΠ°Π² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΡΠΈΠ½Π°
- 2. 3. ΠΠ΅ΡΠΎΠ΄Ρ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠΉ ΡΠ΅ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ ΠΈ ΠΈΠ·ΡΡΠ΅Π½ΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΡΠΈΠ½Π°
- 2. 4. ΠΠΈΠ°ΠΌΠ΅ΡΡ Π²ΠΎΠ΄Π½ΠΎΠΉ ΠΏΠΎΡΡ, ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΡ ΠΏΡΠΎΠ²ΠΎΠ΄ΠΈΠΌΠΎΡΡΠΈ ΠΈ ΠΈΠΎΠ½Π½Π°Ρ ΡΠ΅Π»Π΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΏΠΎΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΠΊΠ°Π½Π°Π»Π°
- 2. 4. 1. ΠΠΈΠ°ΠΌΠ΅ΡΡ Π²ΠΎΠ΄Π½ΠΎΠΉ ΠΏΠΎΡΡ
- 2. 4. 2. ΠΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΠΈ ΠΈ ΡΠ΅Π»Π΅ΠΊΡΠΈΠ²Π½ΡΠΉ ΡΠΈΠ»ΡΡΡ ΠΏΠΎΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΠΊΠ°Π½Π°Π»Π°
- 2. 5. ΠΠΎΡΠΈΠ½-ΡΠ΅ΡΠΌΠ΅Π½ΡΠ½ΡΠ΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΡ
- 2. 6. ΠΠΈΠΎΠ³Π΅Π½Π΅Π· ΠΈ ΡΡΡΠΎΠ΅Π½ΠΈΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΡΠΈΠ½Π°
- 2. 7. ΠΠΎΡΠΈΠ½ ΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΉ Π±Π΅Π½Π·ΠΎΠ΄ΠΈΠ°Π·Π΅ΠΏΠΈΠ½ΠΎΠ²ΡΠΉ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡ
- 2. 8. ΠΡΠΎΠ±Π»Π΅ΠΌΡ, Π²ΠΎΠ·Π½ΠΈΠΊΠ°ΡΡΠΈΠ΅ ΠΏΡΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΡΠΈΠ½Π°
- 3. Π’ΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡ Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠ²ΡΡ
Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ²
- 3. 1. ΠΠΎΠΊΠ°Π»ΠΈΠ·Π°ΡΠΈΡ ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π° ΠΠΠ’
- 3. 2. Π¦ΠΈΠΊΠ» ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ° Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ²
- 3. 3. Π Π΅Π³ΡΠ»ΡΡΠΈΡ ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ° Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ² ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΠΌ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»ΠΎΠΌ
- 3. 4. ΠΠΎΠ΄Π΅Π»ΠΈ, ΠΎΠΏΠΈΡΡΠ²Π°ΡΡΠΈΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΡΡΠ°Π½ΡΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΠΎΠ³ΠΎ ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ°
- 3. 5. ΠΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΡ ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ° Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ² ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠΎΠΌ
- 3. 6. Π‘ΡΡΡΠΊΡΡΡΠ° ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ° Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠ²ΡΡ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ²
- 4. ΠΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π· Π°
- ΠΠ°ΡΠ΅ΡΠΈΠ°Π»Ρ ΠΈ ΠΌΠ΅ΡΠΎΠ΄Ρ
- 1. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 2. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠ³ΠΎ ΡΠΎΡΡΠΎΡΠ½ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 3. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΈΠΈ Π±Π΅Π»ΠΊΠ°
- 4. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠ½Π·ΠΈΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ
- 5. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΏΠΎΡΠΈΠ½Π° ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΠΎΠ΄Π½ΠΎΡΡΡΠΏΠ΅Π½ΡΠ°ΡΠΎΠΉ Π°Π΄ΡΠΎΡΠ±ΡΠΈΠΎΠ½Π½ΠΎΠΉ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΠΈ
- 6. ΠΡΠΈΡΡΠΊΠ° Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² ΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΏΠΎΠ²Π΅Π΄Π΅Π½ΠΈΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ ΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ²
- 7. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠ°Π½Π°Π»ΡΠ½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΏΠΎΡΠΈΠ½Π° Π² ΡΠΎΡΡΠ°Π²Π΅ Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΈ Π΄Π»Ρ ΠΈΠ½Π΄ΠΈΠ²ΠΈΠ΄ΡΠ°Π»ΡΠ½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ°
- 8. Π Π°Π·Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΠΈΠΎΠ½ΠΎΠΎΠ±ΠΌΠ΅Π½Π½ΠΎΠΉ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΠΈ
- 9. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΠΏΠΎΠ»ΠΈΠΊΠ»ΠΎΠ½Π°Π»ΡΠ½ΡΡ Π°Π½ΡΠΈΡΠ΅Π» Π½Π° Π°ΡΡΠ°ΠΊΡΠΈΠ»ΠΎΠ·ΠΈΠ΄-ΡΠ²ΡΠ·ΡΠ²Π°ΡΡΠΈΠΉ ΡΡΠ°ΡΡΠΎΠΊ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ°
- 10. ΠΡΠΈΡΡΠΊΠ° ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ° ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΠΈ Π½Π° ΠΈΠΌΠΌΡΠ½ΠΎΡΠΎΡΠ±Π΅Π½ΡΠ΅
- 11. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠ³ΠΎ Π²Π΅ΡΠ° Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ²
- 12. ΠΠ΄Π΅Π½ΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ²
- 13. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Π-ΠΊΠΎΠ½ΡΠ΅Π²ΠΎΠΉ ΠΏΠΎΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΠ΅Π»ΡΠ½ΠΎΡΡΠΈ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ°, Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΠΎΠ³ΠΎ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΠΈΠΌΠΌΡΠ½ΠΎΡΠΎΡΠ±ΡΠΈΠΈ ΠΈΠ· ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Ρ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·ΠΎΠΉ
- 14. Π€ΡΠ°ΠΊΡΠΈΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΏΠΎΡΠ΅ΠΊ ΠΊΡΡΡΡ ΠΈ ΠΎΡΠΈΡΡΠΊΠ° ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΈΠ· ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ°ΡΡΠΌΠ΅Π½ΡΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ
- 15. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ΅Ρ ΠΈΠΎΠΌΠ΅ΡΡΠΈΠΈ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΏΠ΅ΡΠΈΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΊΠΈΠ½Π°Π· ΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ Π΄Π»Ρ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΈΠ· ΡΠ°Π·Π½ΡΡ ΡΠΊΠ°Π½Π΅ΠΉ
- 16. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΡ Π»ΠΈΠΏΠΈΠ΄ΠΎΠ² Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΈΡΡΠ»Π΅Π΄ΡΠ΅ΠΌΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ²
- 17. ΠΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ ΡΡΠΈΠ²Π°ΡΡΠΈΡ ΡΠ΅Π°Π³Π΅Π½ΡΠΎΠ² Π΄Π»Ρ Π²ΡΠ΄Π΅Π»Π΅Π½ΠΈΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΏΠ΅ΡΠΈΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΊΠΈΠ½Π°Π· ΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ
- 18. ΠΠ·ΠΎΡΠ½Π·ΠΈΠΌΡΠ»Π΅ΠΊΡΡΠΎΡΠΎΡΠ΅Π· ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ Π² ΠΏΠΎΠ»ΡΡΠ΅Π½Π½ΡΡ ΠΏΡΠΎΠ±Π°Ρ
- Π ΠΠΠ£ΠΠ¬Π’ΠΠ’Π« Π ΠΠΠ‘Π£ΠΠΠΠΠΠ― Π€ΡΠ°ΠΊΡΠΈΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΏΠΎΡΠ΅ΠΊ ΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΠ°ΡΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ Π² ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ°ΡΡΠΌΠ΅Π½ΡΠ°Ρ
- 2. ΠΡΠΈΡΡΠΊΠ° ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Π°Π½ΠΈΠΎΠ½ΠΎΠΎΠ±ΠΌΠ΅Π½Π½ΠΎΠΉ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΠΈ
- 3. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠ³ΠΎ ΡΠΎΡΡΠ°Π²Π° ΡΡΠ°ΠΊΡΠΈΠΉ ΡΠ»ΡΠ°ΡΠ° Ρ ΠΠΠΠ ΡΠ΅Π»Π»ΡΠ»ΠΎΠ·Ρ, ΠΎΠ±Π»Π°Π΄Π°ΡΡΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡΡ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ
- 4. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ Π»ΠΈΠΏΠΈΠ΄Π½ΠΎΠ³ΠΎ ΡΠΎΡΡΠ°Π²Π° ΡΡΠ°ΠΊΡΠΈΠΉ Ρ ΠΠΠΠ ΡΠ»Π»ΡΠ»ΠΎΠ·Ρ, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΡ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΠ΅ Π±Π΅Π»ΠΊΠΈ
- 5. Π€ΡΠ°ΠΊΡΠΈΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΌΠΎΠ·Π³Π° Π½Π° ΠΠΠΠ ΡΠ΅Π»Π»ΡΠ»ΠΎΠ·Π΅
- 6. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΎΡΠ½ΠΎΡΠΈΡΠ΅Π»ΡΠ½ΠΎΠΉ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠΉ ΠΌΠ°ΡΡΡ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°Π΅ΠΌΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ²
- 7. ΠΠ΄Π΅Π½ΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΠΈΠ·ΠΎΡΠΎΡΠΌ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ° Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΈΡΡΠ»Π΅Π΄ΡΠ΅ΠΌΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ Π°ΡΡΠΎΡΠΈΠ°ΡΠΎΠ²
- 8. ΠΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠΈΠ²Π°ΡΡΠ΅Π³ΠΎ ΡΠ΅Π°Π³Π΅Π½ΡΠ° ΠΏΡΠΈ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΠΈ ΠΈΡΡΠ»Π΅Π΄ΡΠ΅ΠΌΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΌΠΎΠ·Π³Π°
- 9. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ΅Ρ ΠΈΠΎΠΌΠ΅ΡΡΠΈΠΈ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² ΡΡΠ°ΠΊΡΠΈΠΎΠ½ΠΈΡΡΠ΅ΠΌΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ²
- 10. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ΅Ρ ΠΈΠΎΠΌΠ΅ΡΡΠΈΠΈ Π»ΠΈΠΏΠΈΠ΄ΠΎΠ² Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΈΡΡΠ»Π΅Π΄ΡΠ΅ΠΌΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ²
- 11. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ Π°Π½Π°Π»ΠΈΠ· ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΡΠ»Π΅ΠΊΡΡΠΎΡΠΎΡΠ΅Π·Π° Π² Π½Π°ΡΠΈΠ²Π½ΡΡ ΡΡΠ»ΠΎΠ²ΠΈΡΡ ΠΈ Π² ΠΏΡΠΈΡΡΡΡΡΠ²ΠΈΠΈ Π΄ΠΎΠ΄Π΅ΡΠΈΠ»ΡΡΠ»ΡΡΠ°ΡΠ° Π½Π°ΡΡΠΈΡ
- 12. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π½ΠΎΠΉ ΡΠ΅Π°ΠΊΡΠΈΠΈ Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΌΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΠΌΠΈ Π±Π΅Π»ΠΊΠ°ΠΌΠΈ
- 13. ΠΠ°Π½Π°Π»ΡΠ½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΏΠΎΡΠΈΠ½Π° Π² ΡΠΎΡΡΠ°Π²Π΅ Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° Ρ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·ΠΎΠΉ
- 14. ΠΠ·ΠΎΠ·ΠΈΠΌ-ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΎΠ΅ ΡΠ°ΡΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΠ’Π€/ΠΠΠ€ Π°Π½ΡΠΈΠΏΠΎΡΡΠ΅ΡΠ° Π² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΡΡ ΠΌΠΎΠ·Π³Π° ΠΈ ΠΏΠΎΡΠ΅ΠΊ Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Ρ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·ΠΎΠΉ ΠΈ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·ΠΎΠΉ
- ΠΠ«ΠΠΠΠ«
Π‘ΡΡΡΠΊΡΡΡΠ½ΠΎ-ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΠ΅ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² (ΡΠ΅ΡΠ΅ΡΠ°Ρ, ΠΊΡΡΡΠΎΠ²Π°Ρ, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½ΡΡΠΎΠ»ΡΠ½Π°Ρ)
Π ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΉ Π±ΠΈΠΎΡ ΠΈΠΌΠΈΠΈ ΡΡΠΈΡΠ°Π΅ΡΡΡ ΠΏΠΎΡΡΡΠ»Π°ΡΠΎΠΌ, ΡΡΠΎ ΡΡΠ±ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠ΅ ΡΡΡΡΠΊΡΡΡΡ, Π½Π°Π·ΡΠ²Π°Π΅ΠΌΡΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΡΠΌΠΈ (ΠΈΠ»ΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΌ ΡΠ΅ΡΠΈΠΊΡΠ»ΡΠΌΠΎΠΌ) Π² ΠΊΠ»Π΅ΡΠΊΠ΅ Π²ΡΠΏΠΎΠ»Π½ΡΡΡ ΡΡΠ½ΠΊΡΠΈΡ ΠΎΠΊΠΈΡΠ»Π΅Π½ΠΈΡ ΡΡΠ±ΡΡΡΠ°ΡΠΎΠ², Π² ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠ΅ ΡΠ΅Π³ΠΎ ΡΠΎΠ·Π΄Π°Π΅ΡΡΡ ΡΠ»Π΅ΠΊΡΡΠΎΡ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠΉ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π» ΠΏΡΠΎΡΠΎΠ½ΠΎΠ² ΠΈ Π·Π°ΡΠ΅ΠΌ ΡΠΈΠ½ΡΠ΅Π·ΠΈΡΡΠ΅ΡΡΡ ΠΠ’Π€. ΠΠ΅Π½Π΅ΡΠ°ΡΠΈΡ ΠΏΡΠΎΡΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»Π° ΠΈ ΠΏΠΎΡΠ»Π΅Π΄ΡΡΡΠ°Ρ ΡΡΠ°Π½ΡΡΠΎΡΠΌΠ°ΡΠΈΡ ΡΡΠΎΠ³ΠΎ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»Π° Π΄Π»Ρ ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΠΠ€ ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΡΠ½ΠΊΡΠΈΠ΅ΠΉ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ, ΡΡΠΎ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅ΡΡΡ Π½Π°Π»ΠΈΡΠΈΠ΅ΠΌ ΡΡΡΠ΅ΡΡΠ²Π΅Π½Π½ΡΡ ΡΠ°Π·Π»ΠΈΡΠΈΠΉ Π΄Π²ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΠΊΠ°ΠΊ ΠΏΠΎ ΡΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΡ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² ΠΈ ΠΈΡ Π°Π½ΡΠ°ΠΌΠ±Π»Π΅ΠΉ, ΡΠ°ΠΊ ΠΈ ΠΏΠΎ ΡΠ²ΠΎΠΉΡΡΠ²Π°ΠΌ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠΎΡΡΠΈ Π΄Π»Ρ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ Π½ΠΈΠ·ΠΊΠΎΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ. ΠΠΈΡΡΠ΅Π» ΠΏΠΎΡΡΡΠ»ΠΈΡΠΎΠ²Π°Π», ΡΡΠΎ Π²Π½ΡΡΡΠ΅Π½Π½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ Π½Π΅ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠ° Π΄Π°ΠΆΠ΅ Π΄Π»Ρ ΡΠ°ΠΊΠΈΡ ΠΈΠΎΠ½ΠΎΠ², ΠΊΠ°ΠΊ Π+ ΠΈ ΠΠ" - ΠΈΠ½Π°ΡΠ΅ ΠΏΡΠΎΠΈΡΡ ΠΎΠ΄ΠΈΠ»ΠΎ Π±Ρ ΡΠ°ΡΡΠ΅ΠΈΠ²Π°Π½ΠΈΠ΅ ΠΏΡΠΎΡΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»Π° Π±Π΅Π· ΡΠΈΠ½ΡΠ΅Π·Π° ΠΠ’Π€ (Mitchell and Moyle, 1965) Π ΠΎΡΠ»ΠΈΡΠΈΠ΅ ΠΎΡ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ, Π²Π½Π΅ΡΠ½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠ° Π΄Π»Ρ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²Π° ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠΎΠ² ΠΊΠ»Π΅ΡΠΊΠΈ ΠΈ ΡΡΠ±ΡΡΡΠ°ΡΠΎΠ² ΡΠ΅Π°ΠΊΡΠΈΠΉ, Π»ΠΎΠΊΠ°Π»ΠΈΠ·ΠΎΠ²Π°Π½Π½ΡΡ Π² ΠΌΠ°ΡΡΠΈΠΊΡΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ (Colombini, 1979).
Π ΡΠ²ΡΠ·ΠΈ Ρ ΡΡΠΈΠΌ Π²ΠΎΠ·Π½ΠΈΠΊΠ°Π΅Ρ Π²ΠΎΠΏΡΠΎΡ ΠΎ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠ΅ ΠΎΠ±ΠΌΠ΅Π½Π° ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠ°ΠΌΠΈ ΠΌΠ΅ΠΆΠ΄Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΌ ΠΌΠ°ΡΡΠΈΠΊΡΠΎΠΌ ΠΈ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ.
Π 1979 Π³ΠΎΠ΄Ρ La Noue ΠΈ ΡΠΎΠ°Π²Ρ. (LaNoue and Schoolwerth, 1979) ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Π²Π²Π΅Π΄Π΅Π½ΠΈΡ ΡΠ°Π΄ΠΈΠ°ΠΊΡΠΈΠ²Π½ΠΎΠΉ ΠΌΠ΅ΡΠΊΠΈ Π² ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ, ΡΡΠ°Π½ΡΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΠΉ ΠΏΠ΅ΡΠ΅Π½ΠΎΡ ΠΊΠΎΡΠΎΡΡΡ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°Π»ΡΡ, Π±ΡΠ»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π½ΡΡΡΠ΅Π½Π½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ Π½Π΅ ΡΠ²Π»ΡΠ΅ΡΡΡ Π½Π΅ΠΏΡΠ΅ΠΎΠ΄ΠΎΠ»ΠΈΠΌΡΠΌ ΠΏΡΠ΅ΠΏΡΡΡΡΠ²ΠΈΠ΅ΠΌ Π΄Π»Ρ ΠΎΠ±ΠΌΠ΅Π½Π° ΠΌΠ΅ΠΆΠ΄Ρ ΡΠΈΡΠΎΠ·ΠΎΠ»Π΅ΠΌ ΠΈ ΠΌΠ°ΡΡΠΈΠΊΡΠΎΠΌ. Π§Π΅ΡΠ΅Π· 10 Π»Π΅Ρ ΡΡΠ°Π»ΠΎ ΠΈΠ·Π²Π΅ΡΡΠ½ΠΎ ΠΎ ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΎΠ΄ΠΈΠ½Π½Π°Π΄ΡΠ°ΡΠΈ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌ Π²ΠΎ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ (Kramer and Palmieri, 1989). ΠΠΎΠ΄ΠΎΠ±Π½ΠΎΠ΅ Π΄ΠΎΡΡΠΈΠΆΠ΅Π½ΠΈΠ΅ ΡΡΠ°Π»ΠΎ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΡΠΌ ΠΏΠΎΡΠ»Π΅ ΠΎΠ±Π½Π°ΡΡΠΆΠ΅Π½ΠΈΡ Π² 1984 Π³ΠΎΠ΄Ρ Π²ΡΡΠΎΠΊΠΎΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ ΠΌΠ΅ΡΠΎΠ΄Π° ΡΠ°Π·Π΄Π΅Π»Π΅Π½ΠΈΡ Π±Π΅Π»ΠΊΠΎΠ²-ΠΏΠ΅ΡΠ΅Π½ΠΎΡΡΠΈΠΊΠΎΠ² ΠΏΡΡΠ΅ΠΌ Π°Π΄ΡΠΎΡΠ±ΡΠΈΠΎΠ½Π½ΠΎΠΉ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΠΈ Π½Π° ΡΠΌΠ΅ΡΠΈ ΡΠ΅Π»ΠΈΡΠ° ΠΈ Π³ΠΈΠ΄ΡΠΎΠΊΡΠΈΠ»Π°ΠΏΠ°ΡΠΈΡΠ° ΠΈ ΠΏΠΎΡΠ»Π΅Π΄ΡΡΡΠ΅ΠΉ ΡΠ΅ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΡΠΈΡΡΠ΅ΠΌΡ ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ° Π² Π»ΠΈΠΏΠΎΡΠΎΠΌΠ°Ρ (Kramer and Heberger, 1986), (Nalecz et al., 1986), (Bisaccia et al., 1988) (Stipani and Palmieri, 1983) (Kaplan and Pedersen, 1985), (Bisaccia et al., 1988).
ΠΠ°ΡΠ°Π»Π»Π΅Π»ΡΠ½ΠΎ ΠΏΡΠΎΠ΄ΠΎΠ»ΠΆΠ°Π»ΠΎΡΡ ΠΈΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠΎΡΡΠΈ Π²Π½Π΅ΡΠ½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ. ΠΡΠ»ΠΎ ΠΎΠ±Π½Π°ΡΡΠΆΠ΅Π½ΠΎ, ΡΡΠΎ Π½Π°ΡΡΠΆΠ½Π°Ρ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠ° Π΄Π»Ρ Π³ΠΈΠ΄ΡΠΎΡΠΈΠ»ΡΠ½ΡΡ Π²Π΅ΡΠ΅ΡΡΠ² Ρ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠΉ ΠΌΠ°ΡΡΠΎΠΉ Π΄ΠΎ 3 ΠΊΠΠ° (Holden and Colombini, 1988). ΠΡΠ΄Π²ΠΈΠ³Π°Π²ΡΠ°ΡΡΡ Π² ΡΠΎ Π²ΡΠ΅ΠΌΡ Π³ΠΈΠΏΠΎΡΠ΅Π·Π° ΠΎ Π»ΠΈΠΏΠΈΠ΄Π½ΠΎΠΉ ΠΏΡΠΈΡΠΎΠ΄Π΅ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌ Π½Π΅ ΠΏΠΎΠ»ΡΡΠΈΠ»Π° ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½ΠΈΡ. Π’ΠΎΠ³Π΄Π° ΠΆΠ΅ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½ΠΎΠΉ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΠΈ ΠΈ Π΄ΠΈΡΡΠ°ΠΊΡΠΈΠΈ ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΠ²ΡΠΊΠΈΡ Π»ΡΡΠ΅ΠΉ Π±ΡΠ»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠ΅ Π² Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΡΠ°ΡΡΠ΅Π½ΠΈΠΉ ΠΏΠΎΡΠΎΠΎΠ±ΡΠ°Π·Π½ΡΡ ΡΡΡΡΠΊΡΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠΉ ΠΏΡΠΈΡΠΎΠ΄Ρ Π΄ΠΈΠ°ΠΌΠ΅ΡΡΠΎΠΌ ΠΎΠΊΠΎΠ»ΠΎ 3 Π½ΠΌ. Π₯ΠΎΠ»Π΄Π΅Π½ ΠΈ ΠΠΎΠ»ΠΎΠΌΠ±ΠΈΠ½ΠΈ (Holden and Colombini, 1988) ΠΈ ΡΠΎΠ°Π²Ρ., ΠΈΡΡΠ»Π΅Π΄ΡΡ ΠΏΠ°ΡΡΠΈΠ²Π½ΡΡ Π΄ΠΈΡΡΡΠ·ΠΈΡ ΡΠ΅ΡΠ΅Π· ΠΠΠ, Π²ΡΠ·ΡΠ²Π°Π΅ΠΌΡΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠ°ΠΌΠΈ Π½Π°ΡΡΠΆΠ½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ, ΠΎΠ±Π½Π°ΡΡΠΆΠΈΠ»ΠΈ Π½Π°Π»ΠΈΡΠΈΠ΅ ΡΠ»Π°Π±ΠΎ ΡΠ΅Π»Π΅ΠΊΡΠΈΠ²Π½ΡΡ Π°Π½ΠΈΠΎΠ½Π½ΡΡ ΠΊΠ°Π½Π°Π»ΠΎΠ² Ρ Π²ΡΡΠ°ΠΆΠ΅Π½Π½ΠΎΠΉ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΡΡ ΠΏΡΠΎΠ²ΠΎΠ΄ΠΈΠΌΠΎΡΡΠΈ. ΠΠ΅Π»ΠΎΠΊ, ΡΠ²Π»ΡΡΡΠΈΠΉΡΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠΌ Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΈ ΠΏΡΠΈ Π²ΡΡΡΠ°ΠΈΠ²Π°Π½ΠΈΠΈ Π² Π»ΠΈΠΏΠΎΡΠΎΠΌΡ ΠΈ ΠΠΠ ΠΎΠ±ΡΠ°Π·ΡΡΡΠΈΠΉ ΠΊΠ°Π½Π°Π»Ρ (ΠΏΠΎΡΡ) Π΄ΠΈΠ°ΠΌΠ΅ΡΡΠΎΠΌ 2 Π½ΠΌ, ΠΏΠΎΠ»ΡΡΠΈΠ» Π½Π°Π·Π²Π°Π½ΠΈΠ΅ «ΠΏΠΎΡΠΈΠ½» ΠΏΠΎ Π°Π½Π°Π»ΠΎΠ³ΠΈΠΈ Ρ ΡΠΆΠ΅ ΠΈΠ·Π²Π΅ΡΡΠ½ΡΠΌ Π±Π΅Π»ΠΊΠΎΠΌ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΏΡΠΈΡΠΎΠ΄Ρ ΡΠΎ ΡΡ ΠΎΠΆΠΈΠΌΠΈ ΡΡΠ½ΠΊΡΠΈΡΠΌΠΈ.
ΠΠ° ΠΎΡΠ½ΠΎΠ²Π°Π½ΠΈΠΈ ΡΡΠΈΡ Π΄Π°Π½Π½ΡΡ Π±ΡΠ»ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΎ, ΡΡΠΎ Π΄ΠΈΡΡΡΠ·ΠΈΡ ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠΎΠ² ΡΠ΅ΡΠ΅Π· Π½Π°ΡΡΠΆΠ½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ Π½Π΅ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΎΠ³ΡΠ°Π½ΠΈΡΠΈΠ²Π°ΡΡΠΈΠΌ ΡΠ°ΠΊΡΠΎΡΠΎΠΌ Π΄Π»Ρ ΡΠΊΠΎΡΠΎΡΡΠ΅ΠΉ ΠΎΠΊΠΈΡΠ»ΠΈΡΠ΅Π»ΡΠ½ΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ Π² ΠΌΠ°ΡΡΠΈΠΊΡΠ΅. Π ΡΠΎ ΠΆΠ΅ Π²ΡΠ΅ΠΌΡ Brdiczka ΠΈ ΡΠΎΠ°Π²Ρ. (Brdiczka and Kolb, 1978) ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π»ΠΈ ΠΊΠΈΠ½Π΅ΡΠΈΠΊΡ ΠΎΠ±ΠΌΠ΅Π½Π° ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠ°ΠΌΠΈ ΠΌΠ΅ΠΆΠ΄Ρ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠΎΠΉ ΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ΅ΠΉ ΠΈ ΠΏΠΎΠΊΠ°Π·Π°Π»ΠΈ, ΡΡΠΎ Π½Π°ΡΡΠΆΠ½Π°Ρ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° Π·Π°ΠΌΠ΅ΡΠ½ΠΎ ΠΎΠ³ΡΠ°Π½ΠΈΡΠΈΠ²Π°Π΅Ρ ΠΏΡΠΎΠ½ΠΈΠΊΠ½ΠΎΠ²Π΅Π½ΠΈΠ΅ ΡΡΠ±ΡΡΡΠ°ΡΠΎΠ² ΠΊ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΌ ΠΌΠ΅ΠΆΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΠΎΠ³ΠΎ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π°.
ΠΠΏΠΎΡΠ»Π΅Π΄ΡΡΠ²ΠΈΠΈ Π±ΡΠ»ΠΎ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ (Mannella and Wang, 1989), ΡΡΠΎ ΠΊΠ°Π½Π°Π», ΠΎΠ±ΡΠ°Π·ΡΠ΅ΠΌΡΠΉ ΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΏΡΠΈ Π²ΡΡΡΠ°ΠΈΠ²Π°Π½ΠΈΠΈ Π² ΠΠΠ, Π½Π΅ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌ Π΄Π»Ρ Π½Π΅ΠΊΠΎΡΠΎΡΡΡ ΠΊΠ°ΡΠΈΠΎΠ½ΠΎΠ² Ρ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠΉ ΠΌΠ°ΡΡΠΎΠΉ ΠΎΠΊΠΎΠ»ΠΎ 400 ΠΠ° ΠΏΡΠΈ ΡΠΎΡ ΡΠ°Π½Π΅Π½ΠΈΠΈ Π²ΡΡΠΎΠΊΠΎΠΉ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠΎΡΡΠΈ Π΄Π»Ρ Π΄ΡΡΠ³ΠΈΡ Π²Π΅ΡΠ΅ΡΡΠ² Ρ ΠΌΠ°ΡΡΠΎΠΉ Π΄ΠΎ 3 ΠΊΠΠ°. Π’Π°ΠΊΠΈΠΌ ΠΎΠ±ΡΠ°Π·ΠΎΠΌ, Π² ΠΊΠΎΠ½ΡΠ΅ 80-Ρ Π³ΠΎΠ΄ΠΎΠ² ΡΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π»ΠΎΡΡ ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»Π΅Π½ΠΈΠ΅ ΠΎ ΡΠΎΡΠ΅ΡΠ°Π½ΠΈΠΈ Π΄Π»Ρ Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΡΠ²ΠΎΠΉΡΡΠ² Π²ΡΡΠΎΠΊΠΎΠΉ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠΎΡΡΠΈ Π΄Π»Ρ ΠΎΠ΄Π½ΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ ΠΈ ΠΈΠ·Π±ΠΈΡΠ°ΡΠ΅Π»ΡΠ½ΠΎΡΡΠΈ Π² ΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΠΈ Π΄ΡΡΠ³ΠΈΡ : Π½Π°ΡΡΠΆΠ½Π°Ρ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° Π½Π΅ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΏΠ°ΡΡΠΈΠ²Π½ΡΠΌ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠΌ ΡΠΈΡΠΎΠΌ, Π° ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»ΡΠ΅Ρ ΡΠΎΠ±ΠΎΠΉ ΡΠ΅Π³ΡΠ»ΠΈΡΡΠ΅ΠΌΡΡ ΡΠΈΡΡΠ΅ΠΌΡ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ° ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠΎΠ², ΡΠ΅Π°Π»ΠΈΠ·ΡΡ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΏΠΎΡΠΎΠΊ Π²Π΅ΡΠ΅ΡΡΠ² ΠΈ ΠΈΠ½ΡΠΎΡΠΌΠ°ΡΠΈΠΈ ΠΌΠ΅ΠΆΠ΄Ρ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ΅ΠΉ ΠΈ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠΎΠΉ.
ΠΠ·Π»ΠΎΠΆΠ΅Π½Π½ΠΎΠ΅ Π²ΡΡΠ΅ ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»Π΅Π½ΠΈΠ΅ ΠΈΠΌΠ΅Π΅Ρ ΠΏΡΠ°Π²ΠΎ Π½Π° ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΏΡΠΈ ΡΡΠ»ΠΎΠ²ΠΈΠΈ ΡΠ΅ΡΠΊΠΎΠΉ ΠΊΠΎΠΌΠΏΠ°ΡΡΠΌΠ΅Π½ΡΠ°Π»ΠΈΠ·Π°ΡΠΈΠΈ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΈ Π²Π½Π΅ΡΠ½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½, ΠΏΠΎΡΠΊΠΎΠ»ΡΠΊΡ ΠΏΡΠΈ ΠΈΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ΅ ΠΌΠΎΠΆΠ΅Ρ ΠΏΡΠΎΠΈΠ·ΠΎΠΉΡΠΈ Π΄ΠΈΡΡΠΈΠΏΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΏΠΎΡΠ΅Π½ΡΠΈΠ°Π»Π° Π½Π° Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅, ΡΡΠΎ Ρ ΡΠΎΡΠΊΠΈ Π·ΡΠ΅Π½ΠΈΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΠΎΠΉ ΡΠ½Π΅ΡΠ³Π΅ΡΠΈΠΊΠΈ, ΡΠ΄Π΅Π»Π°Π΅Ρ Π΅Π΅ Π±Π΅ΡΡΠΌΡΡΠ»Π΅Π½Π½ΠΎΠΉ Π΄Π»Ρ ΡΠΈΠ½ΡΠ΅Π·Π° ΠΠ’Π€.
Π ΡΠΎ ΠΆΠ΅ Π²ΡΠ΅ΠΌΡ ΠΈΠ·Π²Π΅ΡΡΠ½ΠΎ, ΡΡΠΎ ΠΏΠΎΠ΄ΠΎΠ±Π½ΡΠ΅ ΠΊΠΎΠ½ΡΠ°ΠΊΡΡ ΡΡΡΠ΅ΡΡΠ²ΡΡΡ ΠΈ Π½ΠΎΡΡΡ Π½Π°Π·Π²Π°Π½ΠΈΠ΅ contact-sites (Hackenbrock, 1968) (Brdiczka and Kolb, 1978). Π₯Π°ΠΊΠ΅Π½Π±ΡΠΎΠΊ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π» ΡΠΎΠ½ΠΊΠΈΠ΅ ΡΡΠ΅Π·Ρ ΡΠΈΠΊΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½ΠΎΠΉ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΠΈ ΠΈ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΠΈΠ», ΡΡΠΎ ΡΠΈΡΠ»ΠΎ ΠΌΠ΅ΠΆΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠΎΠ² Π΄ΠΎΡΡΠΈΠ³Π°Π΅Ρ 120 Π½Π° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΡ ΡΡΠ΅Π΄Π½Π΅Π³ΠΎ ΡΠ°Π·ΠΌΠ΅ΡΠ° ΠΎΠΊΠΎΠ»ΠΎ 1ΠΌΠΊΠΌ ΠΈ Π·ΠΎΠ½Π° ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ° ΠΈΠΌΠ΅Π΅Ρ Π΄ΠΈΠ°ΠΌΠ΅ΡΡ Π΄ΠΎ 200 Π. ΠΠΊΠ°Π·Π°Π»ΠΎΡΡ, ΡΡΠΎ Π²Π½ΡΡΡΠ΅Π½Π½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π° Π½Π΅ΠΎΠ΄Π½ΠΎΡΠΎΠ΄Π½Π° ΠΈ ΡΠΎΡΡΠΎΠΈΡ ΠΈΠ· ΡΠ²ΡΠ·ΡΡΡΠ΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ (inner boundary membrane), ΠΊΠΎΠ½ΡΠ°ΠΊΡΠΈΡΡΡΡΠ΅ΠΉ Ρ Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ΠΎΠΉ, ΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΊΡΠΈΡΡ (crystae-membrane), Π½Π΅ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠΈΡΡΡΡΠ΅ΠΉ Ρ Π²Π½Π΅ΡΠ½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ΠΎΠΉ. ΠΠΎ ΠΎΠ΄Π½ΠΎΠΉ ΠΌΠΎΠ΄Π΅Π»ΠΈ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°Π΅ΡΡΡ, ΡΡΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΡΠ²ΡΠ·ΡΡΡΠ΅ΠΉ ΠΈ Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΏΡΠΎΠΈΡΡ ΠΎΠ΄ΠΈΡ ΡΠ΅ΡΠ΅Π· ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠΈΠ»Π°ΠΌΠΈΠ½Π°ΡΠ½ΠΎΠΉ ΡΡΡΡΠΊΡΡΡΡ — ΡΠ»ΠΈΠ²Π°ΡΡΡΡ Π²Π½Π΅ΡΠ½ΠΈΠΉ ΠΌΠΎΠ½ΠΎΡΠ»ΠΎΠΉ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΈ Π²Π½ΡΡΡΠ΅Π½Π½ΠΈΠΉ ΠΌΠΎΠ½ΠΎΡΠ»ΠΎΠΉ Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ (Van Venetie and Verkleij, 1982). ΠΠ΄Π½Π°ΠΊΠΎ, Π΄Π°Π½Π½ΡΠ΅ ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΡΡΡΡΠΊΡΡΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΠΈΠ·Π° ΠΏΠΎΡΠΈΠ½Π° Π½Π΅ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π°ΡΡ ΡΡΠΎΠ³ΠΎ ΠΈ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²ΠΎ ΡΠΊΠ»ΠΎΠ½ΡΡΡΡΡ ΠΊ Π±ΠΎΠ»Π΅Π΅ ΠΎΠ±ΠΎΡΠ½ΠΎΠ²Π°Π½Π½ΠΎΠΉ ΡΠΎ ΡΡΡΡΠΊΡΡΡΠ½ΠΎΠΉ ΡΠΎΡΠΊΠΈ Π·ΡΠ΅Π½ΠΈΡ ΠΊΠΎΠ½ΡΠ΅ΠΏΡΠΈΠΈ ΠΡΠ΄ΠΈΡΠΊΠΈ ΠΈ ΡΠΎΠ°Π²ΡΠΎΡΠΎΠ² ΠΎ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΠΌ, Π½ΠΎ Π½Π΅ ΠΎΠ±ΡΠ·Π°ΡΠ΅Π»ΡΠ½ΠΎΠΌ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ΅ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΈ ΠΏΡΠ΅Π²Π°Π»ΠΈΡΠΎΠ²Π°Π½ΠΈΠΈ ΡΠΎΠ»ΠΈ Π±Π΅Π»ΠΎΠΊ-Π±Π΅Π»ΠΊΠΎΠ²ΡΡ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠΉ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΠΎΠ³ΠΎ ΡΠ°ΠΉΡΠ°, ΡΡΠ°Π±ΠΈΠ»ΠΈΠ·ΠΈΡΡΡΡΠΈΡ ΡΡΠ°ΡΡΠΎΠΊ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ° Π΄Π²ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ (Ohlendieck et al., 1986) (Kottke et al., 1988) (Brdiczka, 1994) (Beutneret al., 1996).
Π‘ΠΎΠ³Π»Π°ΡΠ½ΠΎ ΠΠΎΡΠ±Π°Π½ΠΈ ΠΈ ΡΠΎΠ°Π²ΡΠΎΡΠ°ΠΌ (Dorbani et al., 1987) Π² Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΡΡΡΠ΅ΡΡΠ²ΡΠ΅Ρ Π΄Π²Π΅ ΠΏΠΎΠΏΡΠ»ΡΡΠΈΠΈ ΠΏΠΎΡΠΈΠ½Π°: ΠΊΠ°Π½Π°Π»ΠΎΡΠΎΡΠΌΠ΅Ρ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½ΡΡ ΡΡΠ°ΡΡΠΊΠΎΠ² ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΈ ΠΏΠΎΡΠΈΠ½, Π²Ρ ΠΎΠ΄ΡΡΠΈΠΉ Π² ΡΠΎΡΡΠ°Π² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ².
Π‘ Π΄ΡΡΠ³ΠΎΠΉ ΡΡΠΎΡΠΎΠ½Ρ, Π₯Π°ΠΊΠ΅Π½Π±ΡΠΎΠΊ Π΅ΡΠ΅ Π² 1968 Π²ΡΠ΄Π²ΠΈΠ½ΡΠ» ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΈΠ΅, ΡΡΠΎ Π²ΠΎ-ΠΏΠ΅ΡΠ²ΡΡ : ΠΎΠ±ΠΌΠ΅Π½ ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠ°ΠΌΠΈ ΠΌΠ΅ΠΆΠ΄Ρ ΠΌΠ°ΡΡΠΈΠΊΡΠΎΠΌ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΠΈ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠΎΠΉ ΠΏΡΠΎΠΈΡΡ ΠΎΠ΄ΠΈΡ Π² ΠΎΠ±Π»Π°ΡΡΠΈ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ° Π΄Π²ΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π²ΠΎ-Π²ΡΠΎΡΡΡ : ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡ Π°Π΄Π΅Π½ΠΈΠ»ΠΎΠ²ΡΡ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ² Π»ΠΎΠΊΠ°Π»ΠΈΠ·ΠΎΠ²Π°Π½ Π²ΠΎ Π²Π½ΡΡΡΠ΅Π½Π½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ Π² ΡΠΎΠΌ ΠΌΠ΅ΡΡΠ΅, Π³Π΄Π΅ ΠΎΠ½Π° ΠΊΠΎΠ½ΡΠ°ΠΊΡΠΈΡΡΠ΅Ρ Ρ Π²Π½Π΅ΡΠ½Π΅ΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ΠΎΠΉΠ²-ΡΡΠ΅ΡΡΠΈΡ : Π½Π΅ΠΊΠΎΡΠΎΡΡΠ΅ ΠΊΠΈΠ½Π°Π·Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎ ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΡΡΡ Π² ΠΎΠ±Π»Π°ΡΡΠΈ ΡΡΠΈΡ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠΎΠ² (ΠΠ°ΡΠΊΠ΅ΠΏΠ¬Π³ΠΎΡΠΊ, 1968). Π Π°Π±ΠΎΡΡ ΠΠΎΡΠ±Π°Π½ΠΈ ΠΈ ΡΠΎΠ°Π²ΡΠΎΡΠΎΠ² ΡΠ²ΠΈΠ΄Π΅ΡΠ΅Π»ΡΡΡΠ²ΡΡΡ ΠΎ ΠΏΡΠ°Π²ΠΈΠ»ΡΠ½ΠΎΡΡΠΈ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΈΡ Π₯Π°ΠΊΠ΅Π½Π±ΡΠΎΠΊΠ° ΠΎΡΠ½ΠΎΡΠΈΡΠ΅Π»ΡΠ½ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΊΠΈΠ½Π°Π· ΠΈ ΠΏΠΎΡΠΈΠ½Π° — Ρ ΠΊΠ°Π½Π°Π»ΠΎΡΠΎΡΠΌΠ΅ΡΠΎΠΌ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½ΡΡ ΡΡΠ°ΡΡΠΊΠΎΠ² Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΡΠ΅Ρ Π³Π»ΡΡΠ°ΡΠΈΠΎΠ½ΡΡΠ°Π½ΡΡΠ΅ΡΠ°Π·Π°, Π° Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π° ΠΈ Π³Π»ΠΈΡΠ΅ΡΠΎΠ»ΠΊΠΈΠ½Π°Π·Π° ΡΠ²ΡΠ·ΡΠ²Π°ΡΡΡΡ Ρ ΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ², ΠΏΡΠΈΡΠ΅ΠΌ Ρ ΠΎΠ΄Π½ΠΈΠΌ ΠΈ ΡΠ΅ΠΌ ΠΆΠ΅ ΡΡΠ°ΡΡΠΊΠΎΠΌ, ΡΡΠΎ ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΠ»ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠΈΡΡ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΠ·ΠΌΠ° ΡΠ³Π»Π΅Π²ΠΎΠ΄ΠΎΠ² ΠΏΠΎΡΡΠ΅Π΄ΡΡΠ²ΠΎΠΌ ΡΡΠΎΠ³ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠΈΡΠΊΠ»ΡΡΠ°ΡΡΠ΅Π³ΠΎ ΡΠ²ΡΠ·ΡΠ²Π°Π½ΠΈΡ (Kaneko et al., 1985). Π€Π΅Π»ΡΠ³Π½Π΅ΡΠΎΠΌ ΠΈ ΡΠΎΠ°Π²ΡΠΎΡΠ°ΠΌΠΈ Π±ΡΠ»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠ΅ Π² Π½Π°ΡΡΠΆΠ½ΠΎΠΉ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ ΠΠΠΊΠΠ° Π±Π΅Π»ΠΊΠ°, ΡΠ²ΡΠ·ΡΠ²Π°ΡΡΠ΅Π³ΠΎ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ (Feigner et al., 1979). ΠΠΏΠΎΡΠ»Π΅Π΄ΡΡΠ²ΠΈΠΈ ΠΠΈΠ½Π΄Π΅Π½ ΠΈ Π€ΠΈΠ΅ΠΊ Ρ ΡΠΎΠ°Π²ΡΠΎΡΠ°ΠΌΠΈ ΠΏΠΎΠΊΠ°Π·Π°Π»ΠΈ ΡΠΎΠΆΠ΄Π΅ΡΡΠ²Π΅Π½Π½ΠΎΡΡΡ ΡΡΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ° ΠΏΠΎΡΠΈΠ½Ρ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² (Linden et al., 1984Π°) (Fiek et al., 1982).
ΠΠ±Π½Π°ΡΡΠΆΠ΅Π½ΠΈΠ΅ ΡΠ²ΡΠ·ΡΠ²Π°Π½ΠΈΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ Ρ ΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΠ»ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠΈΡΡ ΠΈ Π²ΠΏΠΎΡΠ»Π΅Π΄ΡΡΠ²ΠΈΠΈ ΠΡΠ΄ΠΈΡΠΊΠΎΠΉ (Ohlendieck et al., 1986) Π±ΡΠ»ΠΎ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΠΎ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½ΠΎ, ΡΡΠΎ Π³Π»ΡΠΊΠΎΠ·Π° ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΠ΅ΡΡΡ Π·Π° ΡΡΠ΅Ρ ΠΠ’Π€, Π²ΡΡ ΠΎΠ΄ΡΡΠ΅Π³ΠΎ ΠΈΠ· ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΡΠ΅ΡΠ΅Π· ΠΏΠΎΡΠΈΠ½ΠΎΠ²ΡΠΉ ΠΊΠ°Π½Π°Π», Π° Π½Π΅ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΠ’Π€. ΠΡΠΎ, Π² ΡΠ²ΠΎΡ ΠΎΡΠ΅ΡΠ΅Π΄Ρ, ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΠ»ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠΈΡΡ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠΉ ΠΈ ΡΡΡΡΠΊΡΡΡΠ½ΠΎΠΉ ΡΠ²ΡΠ·ΠΈ ΠΏΠΎΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΠΊΠ°Π½Π°Π»Π° Ρ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠΎΠΌ Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠ²ΡΡ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ², ΡΡΠΎ ΠΈ Π±ΡΠ»ΠΎ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½ΠΎ ΠΠΈΠ½Π΄Π΅Π½ ΠΈ ΡΠΎΠ°Π²ΡΠΎΡΠ°ΠΌΠΈ (Linden et al., 1989).
ΠΠ°ΡΠΈΠ½Π°Ρ Ρ ΡΡΠΎΠ³ΠΎ ΠΌΠΎΠΌΠ΅Π½ΡΠ°, Π²ΡΠ΄Π²ΠΈΠ³Π°Π²ΡΠ΅Π΅ΡΡ ΡΠ°Π½Π΅Π΅ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΈΠ΅ ΠΎ ΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΠΈ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠ° ΡΠΎΠΏΡΡΠΆΠ΅Π½ΠΈΡ Π³Π»ΠΈΠΊΠΎΠ»ΠΈΠ·Π° ΠΈ ΠΎΠΊΠΈΡΠ»ΠΈΡΠ΅Π»ΡΠ½ΠΎΠ³ΠΎ ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΏΠΎΡΡΠ΅Π΄ΡΡΠ²ΠΎΠΌ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΈ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² Π³Π»ΠΈΠΊΠΎΠ»ΠΈΡΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΏΡΡΠΈ, Π»ΠΎΠΊΠ°Π»ΠΈΠ·ΠΎΠ²Π°Π½Π½ΡΡ Π² ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠ΅, ΠΈΠ½ΡΠ΅Π½ΡΠΈΠ²Π½ΠΎ ΡΠ°Π·ΡΠ°Π±Π°ΡΡΠ²Π°Π΅ΡΡΡ ΠΈ ΠΏΠΎΠ»ΡΡΠ°Π΅Ρ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΠΎΠ΅ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½ΠΈΠ΅ Π² ΡΠ°Π±ΠΎΡΠ°Ρ Π³ΡΡΠΏΠΏΡ ΠΡΠ΄ΠΈΡΠΊΠΈ (Brdiczka, 1991) (Brdiczka, 1994) ΠΈ ΠΠΈΠ»ΡΠΎΠ½Π° (Wilson, 1985) (Wilson, 1989).
ΠΡΡΠΏΠΏΠΎΠΉ ΠΡΠ΄ΠΈΡΠΊΠΈ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Ρ ΠΏΠΎΡΠΈΠ½ΠΎΠ²ΡΠΌ ΠΊΠ°Π½Π°Π»ΠΎΠΌ Π΅ΡΠ΅ ΠΎΠ΄Π½ΠΎΠ³ΠΎ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°, ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ. ΠΡΠΈΡΠ΅ΠΌ ΠΈΠ· Π΄Π²ΡΡ ΡΠΎΡΠΌ — ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ, Π² ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠΈ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° Ρ ΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΏΡΠΈΠ½ΠΈΠΌΠ°Π΅Ρ ΡΡΠ°ΡΡΠΈΠ΅ ΡΠΎΠ»ΡΠΊΠΎ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½Π°Ρ, ΡΡΠΎ ΠΎΠ±ΡΡΡΠ½ΡΠ΅ΡΡΡ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΡΡ ΠΎΠ»ΠΈΠ³ΠΎΠΌΠ΅ΡΠ½ΠΎΠ³ΠΎ ΡΡΡΠΎΠ΅Π½ΠΈΡ ΠΏΠΎΡΠ»Π΅Π΄Π½Π΅ΠΉ (oKTaMep)(Brdiczka et al., 1994).
Π’Π°ΠΊΠΈΠΌ ΠΎΠ±ΡΠ°Π·ΠΎΠΌ, ΠΊ Π½Π°ΡΡΠΎΡΡΠ΅ΠΌΡ ΠΌΠΎΠΌΠ΅Π½ΡΡ ΡΠΆΠ΅ ΠΈΠ·Π²Π΅ΡΡΠ½Π° ΡΠ΅Π»Π°Ρ Π³ΡΡΠΏΠΏΠ° Π±Π΅Π»ΠΊΠΎΠ², ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π΅Π½Π½ΠΎ ΠΈ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎ ΡΠ²ΡΠ·Π°Π½Π½ΡΡ Ρ ΡΡΠ°ΡΡΠΊΠΎΠΌ Π²Π·Π°ΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ Π΄Π²ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ, ΡΠΎΡΡΠ°Π²Π»ΡΡ Π±Π΅Π»ΠΊΠΎΠ²ΡΡ ΠΎΡΠ½ΠΎΠ²Ρ ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΠΎΠ³ΠΎ ΡΠ°ΠΉΡΠ° ΠΈ, Π²Π΅ΡΠΎΡΡΠ½ΠΎ, ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΡΡΡΠΈΡ Π² ΡΠΎΡΡΠ°Π²Π΅ Π΅Π΄ΠΈΠ½ΠΎΠ³ΠΎ ΠΌΡΠ»ΡΡΠΈΠ±Π΅Π»ΠΊΠΎΠ²ΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ°. ΠΠΎΠ΄ΡΠΎΠ±Π½Π°Ρ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊΠ° ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² ΡΡΠΎΠΉ ΡΠΈΡΡΠ΅ΠΌΡ Π±Π΅Π»ΠΊΠΎΠ² Ρ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ½ΡΠΌΠΈ, ΡΠΈΠ½ΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΈΠΌΠΈ ΠΈ ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠ½ΡΠΌΠΈ ΡΡΠ½ΠΊΡΠΈΡΠΌΠΈ Π΄Π°Π½Π° Π² ΡΠ»Π΅Π΄ΡΡΡΠ΅ΠΌ ΡΠ°Π·Π΄Π΅Π»Π΅.
ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«.
1. ΠΠ΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π°.
Π²ΡΠ²ΠΎΠ΄Ρ.
1. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ ΠΎΡΠΈΡΡΠΊΠ° ΡΠ°Π·Π»ΠΈΡΠ½ΡΠΌΠΈ ΠΌΠ΅ΡΠΎΠ΄Π°ΠΌΠΈ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ ΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ Ρ ΠΈΠ½ΡΠ΅Π³ΡΠ°Π»ΡΠ½ΡΠΌΠΈ Π±Π΅Π»ΠΊΠ°ΠΌΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½: ΠΏΠΎΡΠΈΠ½ΠΎΠΌ, ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠΎΠΌ, Π΄ΠΈΠ°Π·Π΅ΠΏΠΈΠ½ΠΎΠ²ΡΠΌ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠΎΠΌ ΠΈ Π±Π΅Π»ΠΊΠΎΠΌ ΠΌΠ°ΡΡΠΈΠΊΡΠ° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΈ ΡΠΈΠΊΠ»ΠΎΡΠΈΠ»Π»ΠΈΠ½ΠΎΠΌ ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠ΄ΠΈΠ»ΠΈ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ ΡΡΠ°Π±ΠΈΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ° Ρ ΠΏΠΎΡΡΠΎΡΠ½Π½ΡΠΌ ΡΠΎΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΠ΅ΠΌ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² ΠΈ ΡΠΎΡ ΡΠ°Π½Π΅Π½ΠΈΠ΅ΠΌ ΠΈΡ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΡ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠ΅ΠΉ.
2. ΠΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Π° ΡΠΎΡΠΌΠΈΡΡΠ΅Ρ Ρ ΠΈΠ½ΡΠ΅Π³ΡΠ°Π»ΡΠ½ΡΠΌΠΈ Π±Π΅Π»ΠΊΠ°ΠΌΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π΄Π²Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ°, ΠΎΡΠ»ΠΈΡΠ°ΡΡΠΈΡ ΡΡ ΠΊΠ°ΠΊ ΠΏΠΎ ΡΠΎΡΡΠ°Π²Ρ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² (ΠΏΠΎΡΠΈΠ½, ΡΠΈΠΊΠ»ΠΎΡΠΈΠ»ΠΈΠ½ ΠΈ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡ Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠ²ΡΡ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ²), ΡΠ°ΠΊ ΠΈ ΠΏΠΎ Π»ΠΎΠΊΠ°Π»ΠΈΠ·Π°ΡΠΈΠΈ Π² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΡΡ (ΠΎΠ΄ΠΈΠ½ Π½Π°Ρ ΠΎΠ΄ΠΈΡΡΡ Π² ΠΊΠΎΠ½ΡΠ°ΠΊΡΠ½ΡΡ ΡΠ°ΠΉΡΠ°Ρ , Π° Π²ΡΠΎΡΠΎΠΉ Π² ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΊΡΠΈΡΡΠ°Ρ ).
3. ΠΠ·ΠΎΠ·ΠΈΠΌ 1 ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ° Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠ²ΡΡ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ΠΎΠ² ΡΠ°ΡΠΏΠΎΠ»Π°Π³Π°Π΅ΡΡΡ Π² ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ°Ρ ΠΊΠΎΠ½ΡΠ°ΠΊΠ½ΡΡ ΡΠ°ΠΉΡΠΎΠ², Π° ΠΈΠ·ΠΎΠ·ΠΈΠΌ 2 — Π² Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠΌ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΊΡΠΈΡΡ.
4. ΠΠΎΠ½ΠΎΠΊΠ°Π½Π°Π»ΡΠ½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΏΠΎΡΠΈΠ½Π° Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΏΠΎΡΠΈΠ½ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ ΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ Π² 10 ΡΠ°Π· Π½ΠΈΠΆΠ΅ ΡΠ°ΠΊΠΎΠ²ΠΎΠΉ Π΄Π»Ρ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½ΠΎΠ³ΠΎ ΠΏΠΎΡΠΈΠ½Π° ΠΈ ΡΠΎΡΡΠ°Π²Π»ΡΠ΅Ρ 0,43 Π½Π‘.
5. ΠΠ΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π° Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΈΠΌΠ΅Π΅Ρ Π² 10−40 ΡΠ°Π· ΠΌΠ΅Π½ΡΡΠ΅Π΅ Π·Π½Π°ΡΠ΅Π½ΠΈΠ΅ Π²Π΅Π»ΠΈΡΠΈΠ½Ρ ΠΊΠΎΠ½ΡΡΠ°Π½ΡΡ ΠΠΈΡ Π°ΡΠ»ΠΈΡΠ° ΡΠ΅ΠΌ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½ΡΠΉ ΡΠ΅ΡΠΌΠ΅Π½Ρ ΠΈ ΡΠΎΡΡΠ°Π²Π»ΡΠ΅Ρ 11 ΠΌΠΊΠ. ΠΠΎΠ½ΡΡΠ°Π½ΡΠ° ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΡ Π΄Π»Ρ ΠΠ΄ΠΠΉΠ Π΄Π»Ρ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° Π² 10 ΡΠ°Π· Π½ΠΈΠΆΠ΅, ΡΠ΅ΠΌ Π΄Π»Ρ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½ΠΎΠΉ ΡΠΎΡΠΌΡ ΠΈ ΡΠΎΡΡΠ°Π²Π»ΡΠ΅Ρ ΠΎΠΊΠΎΠ»ΠΎ 20 ΠΌΠΊΠ.
6. ΠΠ΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Π° ΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Π° Π² ΡΠΎΡΡΠ°Π²Π΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΡΡΡ Π² ΡΠΎΠΏΡΡΠΆΠ΅Π½Π½ΠΎΠΉ ΡΠΈΡΡΠ΅ΠΌΠ΅ ΠΏΠ΅ΡΠ΅Π½ΠΎΡΠ° ΡΠΎΡΡΠΎΡΠΈΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΎΡΡΠ°ΡΠΊΠ° ΠΌΠ΅ΠΆΠ΄Ρ ΠΊΡΠ΅Π°ΡΠΈΠ½ΡΠΎΡΡΠ°ΡΠΎΠΌ/ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΎΠΌ ΠΈ ΠΠΠ€/ΠΠ’Π€ ΠΏΡΠΈ ΡΡΠ°ΡΡΠΈΠΈ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ² ΠΏΠΎΡΠΈΠ½Π° ΠΈ ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΎΡΠ° Π±Π΅Π· Π²ΡΡ ΠΎΠ΄Π° ΠΏΡΠΎΠΌΠ΅ΠΆΡΡΠΎΡΠ½ΡΡ ΠΏΡΠΎΠ΄ΡΠΊΡΠΎΠ² ΠΈΠ· Π²Π½ΡΡΡΠ΅Π½Π½Π΅Π³ΠΎ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π° ΡΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ°ΡΡΠΌΠ΅Π½ΡΠ°.
7. ΠΠ΅Π»ΠΊΠΎΠ²ΡΠ΅ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΡ Π³Π΅ΠΊΡΠΎΠΊΠΈΠ½Π°Π·Ρ ΠΈΠ»ΠΈ ΠΊΡΠ΅Π°ΡΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΠ΅ ΡΠΈΠΊΠ»ΠΎΡΠΈΠ»Π»ΠΈΠ½, ΠΏΡΠΈ ΡΠ΅ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ Π² Π»ΠΈΠΏΠΎΡΠΎΠΌΡ ΠΎΠ±Π»Π°Π΄Π°ΡΡ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡΡ ΠΊ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΡ ΠΌΠ΅Π³Π°ΠΊΠ°Π½Π°Π»Π°, ΡΡΠ²ΡΡΠ²ΠΈΡΠ΅Π»ΡΠ½ΠΎΠ³ΠΎ ΠΊ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΡ Π½Π΅ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΏΡΠΎΠ½ΠΈΡΠ°Π΅ΠΌΠΎΡΡΠΈ, ΡΠΈΠΊΠ»ΠΎΡΠΏΠΎΡΠΈΠ½Ρ Π.
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Adams, V., Bosch, W., Schlegel.J., Wallimann, T., and Brdiczka.D. (1989). Further characterization of contact sites from mitochondria of different tissues: topology of peripheral kinases. Biochim. Biophys. Acta 981, 213−225.
- Aquila.H., Misra, D., Eulitz.M., and Klingenberg.M. (1982). Complete amino acid sequence of the ADP/ATP carrier from beef heart mitochondria. Hoppe Seylers Z Physiol Chem 363, 345−349.
- Ardail.D., Privat.J.P., Egret-Charlier, M., Levrat, C., Lerme.F., and Louisot, P. (1990). Mitochondrial contact sites. Lipid composition and dynamics. J. Biol. Chem 265, 18 797−18 802.
- Arora, K.K., Parry.D.M., and Pedersen.P.L. (1992). Hexokinase receptors: preferential enzyme binding in normal cells to nonmitochondrial sites and in transformed cells to mitochondrial sites. J. Bioenerg. Biomembr. 24, 47−53.
- Asryants.R.A., Duszenkova.l.V., and Nagradova.N.K. (1985). Determination of Sepharose-bound protein with Coomassie brilliant blue G-250. Anal. Biochem. 151, 571−574.
- Banga.J.P., Anderton, B.H., and Roitt.l.M. (1978). Separation of membrane proteins in an undenatured form by isoelectric focusing. Anal. Biochem. 89, 348 354.
- Belousova.LA/., Fedosov.S.N., Orlova.E.V., and Stel’mashchuk.V.Y. (1991). The structural features of beef heart mitochondrial creatine kinase. Biochem. Int. 24, 51−58.
- Belousova.L.V., Lipskaya.T.Y., Temple, V.D., and Rostovtsev.A.P. (1982). ATP-creatine phosphotransferase from beef heart mitochondria. Purification and properties. Adv. Myocardiol. 3, 585−595.
- BeltrandelRio, H. and Wilson, J.E. (1992). Interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation and creatine kinase. Arch. Biochem. Biophys. 299, 116−124.
- Benz, R. (1985). Porin from bacterial and mitochondrial outer membranes. CRC Crit Rev. Biochem. 19, 145−190.
- Benz, R., Kottke, M., and Brdiczka.D. (1990). The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim. Biophys. Acta 1022, 311−318.
- Bessman, S.P. and Carpenter, C.L. (1985). The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem. 54, 831−862.
- Bessman, S.P. and Geiger, P.J. (1981). Transport of energy in muscle: the phosphorylcreatine shuttle. Science 211, 448−452.
- Beutner, G., Ruck, A., Riede.B., Welte.W., and Brdiczka, D. (1996). Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396, 189−195.
- Beyer, K. and Klingenberg, M. (1985). ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance. Biochemistry 24, 3821−3826.
- Bisaccia, F., Indiveri.C., and Palmieri, F. (1988). Purification and reconstitution of two anion carriers from rat liver mitochondria: the dicarboxylate and the 2-oxoglutarate carrier. Biochim. Biophys. Acta 933, 229−240.
- Block, M.R., Lauquin, G. J" and Vignais.P.V. (1983). Use of 3−0-naphthoyladenosine 5'-diphosphate to probe distinct conformational states ofmembrane-bound adenosine 5'- diphosphate/adenosine 5'-triphosphate carrier. Biochemistry 22, 2202−2208.
- Bowen, K.A., Tam, K., and Colombini.M. (1985). Evidence for titratable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC. J. Membr. Bioi. 86, 51−59.
- Brdiczka, D. (1991). Contact sites between mitochondrial envelope membranes. Structure and function in en. Biochim. Biophys. Acta 1071, 291−312.
- Brdiczka, D. (1994). Function of the outer mitochondrial compartment in regulation of energy metabolism. Biochim. Biophys. Acta 1187, 264−269.
- Brdiczka, D., Kaldis.P., and Wallimann.T. (1994). In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J. Biol. Chem. 269, 27 640−27 644.
- Brdiczka, D. and Kolb, V. Reduction of ADP/ATP exchange rates after dissociation of the contact sites between the two boundary membranes in rat liver mitochondria. Hoppe Seylers Z Physiol Chem 359, 1063−1071. 1978. Ref Type: Journal (Full)
- Brustovetsky, N. and Klingenberg, M. (1996). Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+. Biochemistry 35, 84 838 488.
- Bucher, K. (1964). Particularities of the heart as a pump. Z Naturwiss. Med. Grundlagenforsch. 2, 119−131.
- Chance, B., Leigh, J.S., Smith, D.S., Nioka, S., and Clark, B.J. (1986). Phosphorus magnetic resonance spectroscopy studies of the role of mitochondria in the disease process. Ann. N. Y. Acad. Sci. 488, 140−153.
- Cheneval, D., Carafoli.E., Powell, G.L., and Marsh, D. (1989). A spin-label electron spin resonance study of the binding of mitochondrial creatine kinase to cardiolipin. Eur. J. Biochem. 186, 415−419.
- Collings, T.A., Braid, H.L., Greene, W.B., and Wheeler, D.D. (1986). Morphometry and autoradiographic analysis of crude synaptosomal preparations from rat cerebral cortex. Neurochem. Res. 11, 707−721.
- Colombini, M. (1979). A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279, 643−645.
- Colombini, M. (1980). Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane. Ann. N. Y. Acad. Sci. 341, 552−563.
- Colombini, M. (1983). Purification of VDAC (voltage-dependent anion-selective channel) from rat liver mitochondria. J. Membr. Biol. 74, 115−121.
- Colombini, M., Yeung, C.L., Tung, J., and Konig, T. (1987). The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion. Biochim. Biophys. Acta 905, 279−286.
- Crompton, M., Ellinger, H., and Costi, A. (1988). Inhibition by cyclosporin A of a Ca2±dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem. J. 255, 357−360.
- De Pinto, V.D. and Palmieri, F. (1992). Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC). J. Bioenerg. Biomembr. 24, 21−26.
- De, P., V, Prezioso.G., and Palmieri.F. (1987). A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues. Biochim. Biophys. Acta 905, 499−502.
- Doring, C. and Colmbini, M. On the nature of the molecular mechanism underlying the voltage dependence of the channel-forminf protein, voltage-dependent anion-selective channel (VDAC). Biophys.J. 45, 44−46. 1984. Ref Type: Journal (Full)
- Doring, C. and Colombini.M. (1985). The mitochondrial voltage-dependent channel, VDAC, is modified asymmetrically by succinic anhydride. J. Membr. Biol. 83, 87−94.
- Dornan, J., Page, A. P., Taylor, P., Wu, S., Winter, A.D., Husi, H., and Walkinshaw.M.D. (1999). Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans. J. Biol. Chem 274, 34 877−34 883.
- Ellington, W.R. (1989). Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens. J. Exp. Biol. 143, 177 194.
- Eppenberger, H.M., Dawson, D.M., and Kaplan, N.O. (1967). The comparative enzymology of creatine kinases. I. Isolation and characterization from chicken and rabbit tissues. J. Biol. Chem 242, 204−209.
- Erdelt, H., Weidemann, M.J., Buchholz, M., and Klingenberg, M. (1972). Some principle effects of bongkrekic acid on the binding of adenine nucleotides to mitochondrial membranes. Eur. J. Biochem. 30, 107−122.
- Erickson-Viitanen.S., Geiger, P., Yang.W.C., and Bessman.S.P. (1982). The creatine-creatine phosphate shuttle for energy transport- compartmentation of creatine Phosphokinase in muscle. Adv. Exp. Med. Biol. 151, 115−125.
- Feigner, P.L., Messer, J.L., and Wilson, J.E. (1979). Purification of a hexokinase-binding protein from the outer mitochondrial membrane. J. Biol. Chem. 254, 4946−4949.
- Feigner, P.L. and Wilson, J.E. (1977). Effect of neutral salts on the interaction of rat brain hexokinase with the outer mitochrondrial membrane. Arch. Biochem. Biophys. 182, 282−294.
- Fiek, C., Benz.R., Roos.N., and Brdiczka.D. (1982). Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim. Biophys. Acta 688, 429−440.
- Font, B., Vial.C., Goldschmidt, D., Eichenberger.D., and Gautheron, D.C. (1981). Heart mitochondrial creatine kinase solubilization. Effect of mitochondrial swelling and SH group reagents. Arch. Biochem. Biophys. 212, 195−203.
- Freitag, H., Neupert, W., and Benz.R. (1982). Purification and characterisation of a pore protein of the outer mitochondrial membrane from Neurospora crassa. Eur. J. Biochem. 123, 629−636.
- Fritz-Wolf, K., Schnyder.T., Wallimann, T., and Kabsch, W. (1996). Structure of mitochondrial creatine kinase see comments. Nature 381, 341−345.
- Gellerich, F.N., Schlame, M., Bohnensack, R., and Kunz, W. (1987). Dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space of rat-heart mitochondria. Biochim. Biophys. Acta 890, 117−126.
- Guo, X.W., Smith, P.R., Cognon.B., D’Arcangelis, D., Dolginova.E., and Mannella, C.A. (1995). Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane. J. Struct. Biol. 114, 4159.
- Hackenberg, H. and Klingenberg, M. (1980). Molecular weight and hydrodynamic parameters of the adenosine 5'- diphosphate-adenosine 5'-triphosphate carrier in Triton X-100. Biochemistry 19, 548−555.
- Hackenbrock, C.R. (1968). Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sei. U. S. A 61, 598−605.
- Harris, R.A., Farmer, B., and Ozawa, T. (1972). Inhibition of the mitochondrial adenine nucleotide transport system by oleyl CoA. Arch. Biochem. Biophys. 150, 199−209.
- Heidt, H.W. (1972). Energy metabolism in mitochondria. Angew. Chem Int. Ed Engl. 11, 792−798.
- Holden, M.J. and Colombini, M. (1988). The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein. FEBS Lett. 241, 105−109.
- Hovius, R., Lambrechts, H., Nicolay, K., and de Kruijff, B. (1990). Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. Biochim. Biophys. Acta 1021, 217−226.
- Huizing, M., DePinto, V., Ruitenbeek, W., Trijbels, F.J., van den Heuvel.L.P., and Wendel, U. (1996). Importance of mitochondrial transmembrane processes in human mitochondriopathies. J. Bioenerg. Biomembr. 28, 109−114.
- Iyengar, M.R. (1984). Creatine kinase as an intracellular regulator. J. Muscle Res. Cell Motil. 5, 527−534.
- Jacobs, H., Heldt, H.W., and Klingenberg, M. (1964). High activity of creatine kinase in mitochondria from muscle and brain and evidence for a separate mitochondrial isoenzyme of creatine kinase. Biochem. Biophys. Res. Commun. 16, 516−521.
- Jennings, R.B. (1981). Myocardial ischemia: introduction. Am. J. Pathol. 102, 239−240.
- Kammermeier, H. (1987). Interrelationship between the free energy change of ATP-hydrolysis, cytosolic inorganic phosphate and cardiac performance during hypoxia and reoxygenation. Biomed. Biochim. Acta 46, S499-S504.
- Kaneko, M., Kurokawa.M., and lshibashi, S. (1985). Binding and function of mitochondrial glycerol kinase in comparison with those of mitochondrial hexokinase. Arch. Biochem. Biophys. 237, 135−141.
- Kaplan, R.S. and Pedersen.P.L. (1985). Isolation and reconstitution of the n-butylmalonate-sensitive dicarboxylate transporter from rat liver mitochondria. J. Biol. Chem. 260, 10 293−10 298.
- Kinnally, K.W., Zorov.D.B., Antonenko, Y.N., Snyder, S.H., McEnery, M.W., and Tedeschi.H. (1993). Mitochondrial benzodiazepine receptor linked to inner membrane ion channels by nanomolar actions of ligands. Proc. Natl. Acad. Sci. U. S. A 90, 1374−1378.
- Klingenberg, M. (1989). Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270, 1−14.
- Klingenberg.M., Aquila.H., and Riccio.P. (1979). Isolation of functional membrane proteins related to or identical with the ADP, ATP carrier of mitochondria. Methods Enzymol. 56, 407−414.
- Knoll, G. and Brdiczka.D. (1983). Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes. Biochim. Biophys. Acta 733, 102−110.
- Kottke, M" Adams, V., Wallimann.T., Nalam.V.K., and Brdiczka, D. (1991). Location and regulation of octameric mitochondrial creatine kinase in the contact sites. Biochim. Biophys. Acta 1061, 215−225.
- Kottke, M., Wallimann.T., and Brdiczka, D. (1994). Dual electron microscopic localization of mitochondrial creatine kinase in brain mitochondria. Biochem. Med. Metab Biol. 51, 105−117.
- Kramer, R. and Heberger, C. (1986). Functional reconstitution of carrier proteins by removal of detergent with a hydrophobic ion exchange column. Biochim. Biophys. Acta 863, 289−296.
- Kramer, R. and Klingenberg, M. (1982). Electrophoretic control of reconstituted adenine nucleotide translocation. Biochemistry 21, 1082−1089.
- Kramer, R. and Palmieri.F. (1989). Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria. Biochim. Biophys. Acta 974, 1−23.
- Kuby, S.A., Noda, L., and Lardy, H.A. (1954). Adenosinetriphosphate-creatine transphorylase. I. Isolation of crystalline evzyme from rabbit muscle. J. Biol. Chem 209, 191−201.
- Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680−685.
- LaNoue, K.F. and Schoolwerth, A.C. (1979). Metabolite transport in mitochondria. Annu. Rev. Biochem. 48, 871−922.
- Lauquin, G.J. and Vignais.P.V. (1976). Interaction of (3H) bongkrekic acid with the mitochondrial adenine nucleotide translocator. Biochemistry 15, 2316−2322.
- Lawson, J.W. and Veech, R.L. (1979). Effects of pH and free Mg2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions. J. Biol. Chem 254, 6528−6537.
- Lazo, P.A., Sols, A., and Wilson, J.E. (1980). Brain hexokinase has two spatially discrete sites for binding of glucose-6-phosphate. J. Biol. Chem. 255, 7548−7551.
- Lehninger, A.L. (1982). Proton and electric charge translocation in mitochondrial energy transduction. Adv. Exp. Med. Biol. 148, 171−186.
- Levin, R.M., Longhurst, P.A., Levin, S.S., Haugaard, N., and Wein.A.J. (1990). Creatine kinase activity of urinary bladder and skeletal muscle from control and streptozotocin-diabetic rats. Mol. Cell Biochem. 97, 153−159.
- Levitsky, D.O., Levchenko, T.S., Saks, V.A., Sharov, V.G., and Smirnov, V.N. (1978). The role of creatine phosphokinase in supplying energy for the calcium pump system of heart sarcoplasmic reticulum. Membr. Biochem. 2, 81−96.
- Linden, M., Andersson.G., Gellerfors.P., and Nelson, B.D. (1984a). Subcellular distribution of rat liver porin. Biochim. Biophys. Acta 770, 93−96.
- Linden, M., Andersson, G., Gellerfors.P., and Nelson, B.D. (1984b). Subcellular distribution of rat liver porin. Biochim. Biophys. Acta 770, 93−96.
- Linden, M., Gellerfors.P., and Nelson, B.D. (1982). Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett. 141, 189−192.
- Linden, M., Nelson, B.D., Loncar.D., and Leterrier, J.F. (1989). Studies on the interaction between mitochondria and the cytoskeleton. J. Bioenerg. Biomembr. 21, 507−518.
- Lohman, K. (1934). Uber die enzymatische Aufspaltung der Kreatinphosphorsaure- zugleich ein Beitrag zum Chemismus der Muskelkontraktion. Biochem. Z 271, 264−277.
- Mannella, C.A. (1981). Structure of the outer mitochondrial membrane: analysis of X-ray diffraction from the plant membrane. Biochim. Biophys. Acta 645, 33−40.
- Mannella, C.A., Colombini, M., and Frank, J. (1983). Structural and functional evidence for multiple channel complexes in the outer membrane of Neurospora crassa mitochondria. Proc. Natl. Acad. Sci. U. S. A 80, 2243−2247.
- Mannella, C.A., Forte, M., and Colombini.M. (1992). Toward the molecular structure of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 24, 7−19.
- Mannella.C.A. and Wang, Q. (1989). Permeability of the mitochondrial outer membrane to organic cations. Biochim. Biophys. Acta 981, 363−366.
- McCabe.E.R. (1994). Microcompartmentation of energy metabolism at the outer mitochondrial membrane: role in diabetes mellitus and other diseases. J. Bioenerg. Biomembr. 26, 317−325.
- Minajeva, A., Ventura-Clapier, R., and Veksler, V. (1996). Ca2+ uptake by cardiac sarcoplasmic reticulum ATPase in situ strongly depends on bound creatine kinase. Pflugers Arch. 432, 904−912.
- Mirzabekov, T.A. and Ermishkin, L.N. (1989). The gate of mitochondrial porin channel is controlled by a number of negative and positive charges. FEBS Lett. 249, 375−378.
- Mitchell, P. and Moyle, J. (1965). Stoichiometry of proton translocation through the respiratory chain and adenosine triphosphatase systems of rat liver mitochondria. Nature 208, 147−151.
- Mommaerts, W.F. and Wallner, A. (1967). The break-down of adenosine triphosphate in the contraction cycle of the frog sartorius muscle. J. Physiol (Lond) 193, 343−357.
- Montal, M. and Mueller, P. (1972). Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. U. S. A 69, 3561−3566.
- Morel, F., Lauquin, G., Lunardi, J., Duszynski.J., and Vignais.P.V. (1974). An appraisal of the functional significance of the inhibitory effect of long chain acyl-CoAs on mitochondrial transports. FEBS Lett. 39, 133−138.
- Morrison, J.F. and White, A. (1967). Isotope exchange studies of the reaction catalyzed by ATP: creatine phosphotransferase. Eur. J. Biochem. 3, 145−152.
- Muller, M., Moser, R., Cheneval, D., and Carafoli.E. (1985). Cardiolipin is the membrane receptor for mitochondrial creatine Phosphokinase. J. Biol. Chem 260, 3839−3843.
- Nakashima, R.A. (1989). Hexokinase-binding properties of the mitochondrial VDAC protein: inhibition by DCCD and location of putative DCCD-binding sites. J. Bioenerg. Biomembr. 21, 461−470.
- Nalecz, K.A., Bolli.R., Wojtczak.L., and Azzi.A. (1986). The monocarboxylate carrier from bovine heart mitochondria: partial purification and its substrate-transporting properties in a reconstituted system. Biochim. Biophys. Acta 851, 29−37.
- Needels.D.L. and Wilson, J.E. (1983). The identity of hexokinase activities from mitochondrial and cytoplasmic fractions of rat brain homogenates. J. Neurochem. 40, 1134−1143.
- Ohlendieck.K., Riesinger,!., Adams, V., Krause, J., and Brdiczka.D. (1986). Enrichment and biochemical characterization of boundary membrane contact sites from rat-liver mitochondria. Biochim. Biophys. Acta 860, 672−689.
- Parola.A.L., Stump, D.G., Pepperl.D.J., Krueger, K.E., Regan, J.W., and Laird, H.E. (1991). Cloning and expression of a pharmacologically unique bovine peripheral- type benzodiazepine receptor isoquinoline binding protein. J. Biol. Chem. 266, 14 082−14 087.
- Peng, S" Blachly-Dyson, E., Colombini, M., and Forte, M. (1992). Determination of the number of polypeptide subunits in a functional VDAC channel from Saccharomyces cerevisiae. J. Bioenerg. Biomembr. 24, 27−31.
- Pfaff, E. and Klingenberg, M. (1968). Adenine nucleotide translocation of mitochondria. 1. Specificity and control. Eur. J. Biochem. 6, 66−79.
- Rojo, M., Hovius, R., Demel, R., Wallimann, T., Eppenberger, H.M., and Nicolay, K. (1991a). Interaction of mitochondrial creatine kinase with model membranes. A monolayer study. FEBS Lett. 281, 123−129.
- Rojo, M., Hovius, R., Demel, R. A" Nicolay, K., and Wallimann.T. (1991b). Mitochondrial creatine kinase mediates contact formation between mitochondrial membranes. J. Biol. Chem 266, 20 290−20 295.
- Roos, N" Benz.R., and Brdiczka.D. (1982). Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria. Biochim. Biophys. Acta 686, 204−214.
- Rose, I.A. and Warms, J.V. (1967). Mitochondrial hexokinase. Release, rebinding, and location. J. Biol. Chem. 242, 1635−1645.
- Rossi, A.M., Zaccaro, L., Rosselli, F., and Quattrone, C. (1988). Clastogenic effects induced in mice and rats by 1,4-bis2-(3,5- dichloropyridyloxy).-benzene, a phenobarbital-like enzyme inducer and liver tumour promoter. Carcinogenesis 9, 1147−1151.
- Schein, S.J., Colombini.M., and Finkelstein.A. (1976). Reconstitution in planar lipid bilayers of a voltage-dependent anion- selective channel obtained from Paramecium mitochondria. J. Membr. Biol. 30, 99−120.
- Schlame, M. and Augustin, W. (1985). Association of creatine kinase with rat heart mitochondria: high and low affinity binding sites and the involvement of phospholipids. Biomed. Biochim. Acta 44, 1083−1088.
- Schlattner, U., Forstner, M., Eder, M., Stachowiak.O., Fritz-Wolf, K., and Wallimann.T. (1998). Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. Mol. Cell Biochem. 184, 125 140.
- Schnaitman.C. and Greenawalt.J.W. (1968). Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J. Cell Biol. 38, 158−175.
- Schnyder.T., Rojo.M., Furter.R., and Wallimann.T. (1994). The structure of mitochondrial creatine kinase and its membrane binding properties. Mol. Cell Biochem. 133−134, 115−123.
- Schnyder.T., Sargent, D.F., Richmond, T. J., Eppenberger, H.M., and Wallimann, T. (1990). Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle. J. Mol. Biol. 216, 809−812.
- Schutkowski, M., Wollner, S., and Fischer, G. (1995). Inhibition of peptidyl-prolyl cis/trans isomerase activity by substrate analog structures: thioxo tetrapeptide-4-nitroanilides. Biochemistry 34, 13 016−13 026.
- Skowronski.R., Fanestil, D.D., and Beaumont, K. (1988). Photoaffinity labeling of peripheral-type benzodiazepine receptors in rat kidney mitochondria with 3H. PK 14 105. Eur. J. Pharmacol. 148, 187−193.
- Smith, A.D. and Wilson, J.E. (1991). Disposition of mitochondrially bound hexokinase at the membrane surface, deduced from reactivity with monoclonal antibodies recognizing epitopes of defined location. Arch. Biochem. Biophys. 287, 359−366.
- Soboll, S" Brdiczka, D., Jahnke, D., Schmidt, A" Schlattner, U" Wendt, S., Wyss, M., and Wallimann.T. (1999). Octamer-dimer transitions of mitochondrial creatine kinase in heart disease. J. Mol. Cell Cardiol. 31, 857−866.
- Souverijn.J.H., Huisman, L.A., Rosing, J., and Kemp, A., Jr. (1973). Comparison of ADP and ATP as substrates for the adenine nucleotide translocator in rat-liver mitochondria. Biochim. Biophys. Acta 305, 185−198.
- Stachowiak, 0., Dolder, M., and Wallimann, T. (1996). Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer. Biochemistry 35, 15 522−15 528.
- Stachowiak.O., Schlattner, U., Dolder, M., and Wallimann, T. (1998). Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure. Mol. Cell Biochem. 184, 141−151.
- Stipani.l. and Palmieri.F. (1983). Purification of the active mitochondrial tricarboxylate carrier by hydroxylapatite chromatography. FEBS Lett. 161, 269 274.
- Tikhonova.l.M., Andreyev, A. Y., Antonenko, Y., Kaulen, A.D., Komrakov.A.Y., and Skulachev.V.P. (1994). Ion permeability induced in artificial membranes by the ATP/ADP antiporter. FEBS Lett. 337, 231−234.
- Trezeguet, V., Le Saux, A., David, C., Gourdet.C., Fiore, C., Dianoux.A., Brandolin, G., and Lauquin, G.J. (2000). A covalent tandem dimer of the mitochondrial ADP/ATP carrier is functional in vivo. Biochim. Biophys. Acta 1457, 81−93.
- Turner, D.C., Wallimann, T., and Eppenberger, H.M. (1973). A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase. Proc. Natl. Acad. Sei. U. S. A 70, 702−705.
- Van Venetie.R. and Verkleij, A.J. (1982). Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study. Biochim. Biophys. Acta 692, 397−405.
- Vignais, P.V. and Lunardi, J. (1985). Chemical probes of the mitochondrial ATP synthesis and translocation. Annu. Rev. Biochem. 54, 977−1014.
- Viitanen.P.V., Geiger, P.J., Erickson-Viitanen, S., and Bessman.S.P. (1984). Evidence for functional hexokinase compartmentation in rat skeletal muscle mitochondria. J. Biol. Chem 259, 9679−9686.
- Voronova.L.A. and Parshin.A.N. (1976). Isoforms of human and animal tumor hexokinase. Vopr. Onkol. 22, 41−45.
- Wallimann.T., Turner, D.C., and Eppenberger.H.M. (1977). Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle. J. Cell Biol. 75, 297−317.
- Wanders, R.J., Van Roermund.C.W., and Meijer, A.J. (1984). Analysis of the control of citrulline synthesis in isolated rat-liver mitochondria. Eur. J. Biochem. 142, 247−254.
- Watts, D.C. and KumudavalliJ. (1970). Further evidence for the role of the essential thiol groups in adenosine triphosphate-creatine phosphotransferase from a comparison of the human and rabbit enzymes. Biochem. J. 118, 22P-23P.
- Weiler.U., Riesinger,!., Knoll, G., and Brdiczka.D. (1985). The regulation of mitochondrial-bound hexokinases in the liver. Biochem. Med. 33, 223−235.
- White, T.K. and Wilson, J.E. (1987). Rat brain hexokinase: location of the allosteric regulatory site in a structural domain at the N-terminus of the enzyme. Arch. Biochem. Biophys. 259, 402−411.
- Wilson, J. (1985). Regulation of mammalian hexokinase activity. In Regulation in carbohydrate metabolism., R. Beither, ed. Boca Raton), pp. 45−85.
- Wilson, J.E. (1989). Rapid purification of mitochondrial hexokinase from rat brain by a single affinity chromatography step on Affi-Gel blue. Prep. Biochem. 19, 13−21.
- Wirz, T., Brandle, U., Soldati, T" Hossle, J.P., and Perriard, J.C. (1990). A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing. J. Biol. Chem 265, 11 656−11 666.
- Yoshizaki.K., Watari, H., and Radda.G.K. (1990). Role of phosphocreatine in energy transport in skeletal muscle of bullfrog studied by 31P-NMR. Biochim. Biophys. Acta 1051, 144−150.