Azanza J L, Raymond J, Robin J M, Cottin P, Ducastaing A
Biochimie. 1980;62(7):481-6. doi: 10.1016/s0300-9084(80)80065-4.
Experiments have been carried out to explore the proteolytic cleavage of rabbit skeletal myofibrils by a calcium dependent neutral proteinase (CaANP). Polyacrylamide gel elctrophoresis on great slabs showed the ability of CaANP to degrade myofibrils more readily than supposed. Besides the hydrolysis of troponin T and the apparition of degradation product of 30,000 molecular weight, the activity of this enzyme is obvious too on some components of the M-line and on heavy subunits of tropomyosin as well as on three unidentified proteic fractions. The variety of the degradation products which appear suggest that the specificity of CaANP is not as selective as presumed. The participation of this proteinase in the postmorten evolution of muscle and its intervention in the turnover of myofibrillar proteins is discussed.
已经开展了实验来探究钙依赖性中性蛋白酶(CaANP)对兔骨骼肌肌原纤维的蛋白水解切割作用。在大型平板上进行的聚丙烯酰胺凝胶电泳显示,CaANP降解肌原纤维的能力比预期的更强。除了肌钙蛋白T的水解以及30,000分子量降解产物的出现外,这种酶对M线的某些成分、原肌球蛋白的重亚基以及三种未鉴定的蛋白质组分也有明显活性。出现的降解产物的多样性表明,CaANP的特异性并不像推测的那样具有选择性。讨论了这种蛋白酶在肌肉死后演变中的作用及其对肌原纤维蛋白周转的干预。