[Neutral calcium dependent proteinase from rabbit skeletal muscle: activity on myofibrillar proteins].
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.
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D008970:Molecular Weight; D009124:Muscle Proteins; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils; D010447:Peptide Hydrolases / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity; D014335:Tropomyosin
D009124:Muscle Proteins; D014335:Tropomyosin; D010447:Peptide Hydrolases; D002118:Calcium
Protéinase neutre calcium dépendante de muscle squelettique de lapin : activité sur les protéines myofibrillaires.