Action of two alkaline proteases and a trypsin inhibitor from white croaker skeletal muscle (Micropogon opercularis) in the degradation of myofibrillar proteins

FEBS Letters

Busconi, L.¹  Folco, E.J.¹  Sánchez, J.J.¹  Marione, C.¹  Trucco, R.E.¹ 

[1] Institute National de Tecnologia Industrial (INTI), Centra de Investigations de Tecnologia Pesquera (CITEP), Morcela T. de Alvear 1168, 7600 Mar del Plata, Argentina

关键词: Fish muscle;    Proteolysis;    Alkaline protease;    Trypsin inhibitor;    Myofibrillar protein;   

DOI  :  10.1016/0014-5793(84)80944-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The action of two alkaline proteases from white skeletal muscle on myofibrillar proteins is shown. Purified myosin was readily degraded by both proteases, but only protease I was able to degrade myosin heavy chain from actomyosin. The effect of inhibitor on both proteases was also studied. The activity of protease II on azocasein was not affected, while the action of protease I on both azocasein and myosin was inhibited. The implication of proteases and inhibitor on the turnover of myofibrillar proteins is considered.

【 授权许可】

Unknown