ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Two proteinases (A and B) were isolated from Atlantic menhaden muscle with molecular weights of 112,000 and 90,500 daltons, respectively. Proteinase B had higher activity than A for protein substrates except casein; proteinase B had no caseinolytic activity. Both proteinases hydrolyzed synthetic substrates such as Z-Phe-Arg-NMecand TAME, but not BAEE and BAPNA. Optimum Z-Phe-Arg-NMec hydrolyzing activity was shown at pH 7.4, 40 to 50 °C for both proteinases A and B. Activities of A and B in the presence of 3.0% NaCl were reduced to 71.2% and 62.2%, respectively. Both proteinases were inhibited by 1 mM TLCK, 1 mM benzamidine, 1% egg white, and 1% bovine plasma hydrolysate. Proteinases A and B are most likely tryptic serine type proteinases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1999.tb15909.x
Permalink