한국식품과학회지 (Korean Journal of Food Science and Technology)
- 제6권2호
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- Pages.79-85
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- 1974
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- 0367-6293(pISSN)
근원섬유 단백질에 관한 연구 (제1보) 근원섬유에 관한 형태학적 연구
Studies on the Myofibrillar Proteins Part I. Phase Microscopy of Myofibrils from Rabbit Muscle
- Yang, Ryung (Department of Food Engineering, College of Science and Engineering, Yon Sei University) ;
- Kim, Chul-Jai (Department of Food Engineering, College of Science and Engineering, Yon Sei University) ;
- Moon, Yoon-Hee (Department of Food Engineering, College of Science and Engineering, Yon Sei University) ;
- Yu, Ju-Hyun (Department of Food Engineering, College of Science and Engineering, Yon Sei University)
- 발행 : 1974.06.28
초록
근원섬유단백질의 생화학적 성질에 대하여서는 아직도 불명한 점이 많고, 특히 식품으로써의 근원섬유단백질의 저장 중의 변화에 대하여서는 규명되어야 할 점이 너무나 많다. 본 연구는 근원섬유단백질의 저장 중의 변화를 추구하기 위한 기초작업으로서 subcelular structure인 근원섬유를 재료로 하여 그 형태학적 측면과 생화학적 측면의 상관성을 비교 검토하였다. 근원섬유의 조제방법에 따라서 근원섬유의 근절(筋節)(sarcomere)의 길이는 변화하고 있었고 근절의 길이의 변화는 생화학적 성질. 즉 ATPase활성에 현저한 변화를 일으켰다. 근원섬유를 저농도의 trypsin으로 처리하면 근원섬유의 ATPase활성은 현저히 증가하나, 근원섬유의 위상차(位相差)현미경 상은 수축상태의 상을 나타내었다가 처리시간의 연장에 따라 sarcomere가 fragmentation을 나타냄을 보여주었다. 얻어진 결과로 근원섬유 중에는 ATPase활성을 저해하는 factor가 존재하며, 이 factor는 단백질의 inhibitory action은 아니고 steric effect임을 추정하였다. 또한 Z-line의 구성물질 중에 troponin의 관여가 추정되었다.
To obtain further information concerning the nature myofibrillar proteins in a food system, an investigation has been conducted to compare the change in the biochemical property of the myofibril with the changes in the morphological structure of the myofibril. When myofibrils were prepared with 0.16 M KCl-0.04 M Tris-HCl, the band pattern was clear and distinct. There was a uniform thickening of A-band, a sharp appearence of Z-lines and a wide I-band. The band pattern of myofibrils was changed as the composition of extraction solution was changed. Also the ATPase activity of myofibril changed as the length of sarcomere changed. When myofibrils were treated with a low concentration of trypsin, myofibrils turned in the contracted state. With the progress of prolonged trypsin treatment, most of myofibrils exhibited a pattern of alternating light and dark bands, supercontracted pattern. Although myofibrils exhibited a supercontracted band pattern, the ATPase activity of myofibril continued to increase with the progress of trypsin treatment. An assumption was made that tropomyosin may be located in Z-line and that troponin-tropomyosin complex can inhibit the ATPase activity of myofibrils through the structural alternation of myofibril.
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