Identification of two alkaline proteases and a trypsin inhibitor from muscle of white croaker (Micropogon opercularis)

FEBS Letters

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

[1] Instituto National de Tecnologia Industrial (INTI), Centro de Investigaciones de Tecnología Pesquera (CITEP), Marcela T. de Alvear 1168, 7600 Mar del Plata, Argentina

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

DOI  :  10.1016/0014-5793(84)80943-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Extracts from white croaker skeletal muscle showed two alkaline proteases and a trypsin inhibitor when they were chromatographed in DEAE-Sephacel. The activity against azocasein was maximal at pH 8.5 and 9.1 for proteases I and II, respectively. Both enzymes showed optimum activity at 60° C. The molecular masses were found to be 132 kDa for protease 1,363 kDa for protease II, and 65 kDa for the inhibitor. Protease I showed the characteristics of a trypsin-like enzyme, and protease II those of a SH-enzyme. These proteins may play important roles in mechanisms of cellular proteolysis.

【 授权许可】

Unknown