PMID: 9442919Jan 27, 1998Paper

Identification of an "alcohol dehydrogenase-activating" protease in grass carp hepatopancreas as a chymotrypsin

Biochemistry and Molecular Biology International
K K LauW P Fong

Abstract

Previous investigation [Tsui et al. (1996) Biochim. Biophys. Acta 1269: 41-46] showed that two active forms of alcohol dehydrogenase can be purified from grass carp. The use of a protease inhibitor and the results of SDS-PAGE analysis of the enzymes suggest that one form (ADH-C) is a proteolytic product of the other (ADH-I). In this study, the protease responsible for the cleavage was purified. The cleavage enzyme had a subunit molecular weight of 28 kDa. An inhibitor study identified it as a serine protease. It exhibited a strong chymotrypsin activity in both esterase and amidase assays with a pH optimum in the range 7.5-8.5. The purified chymotrypsin also cleaved the intact grass carp ADH-I into the two-fragment ADH-C, with an accompanying increase in enzyme activity. A similar effect was not found using horse liver alcohol dehydrogenase.

Citations

Dec 24, 2015·International Journal of Molecular Sciences·Jin-Song GongJin-Song Shi

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