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Hydrolytic Enzymes in Bovine Skeletal Muscle. 3. Activity of Some Catheptic Enzymes
Author(s) -
LUTALOBOSA A. J.,
MACRAE H. F.
Publication year - 1969
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1969.tb12789.x
Subject(s) - cathepsin , enzyme , skeletal muscle , biochemistry , substrate (aquarium) , chemistry , incubation , cathepsin d , proteolytic enzymes , hydrolysis , biology , endocrinology , ecology
SUMMARY: The present study was undertaken to examine the effects of pH, substrate concentration, time of incubation and temperature on proteolytic activity in the skeletal muscle of the bovine and to determine in this tissue enzymatic activities resembling those of cathepsins B, C and D. Maximal proteolytic activity was observed at either pH 3.8 or at pH 4.8 depending upon the enzyme studied. Activities of cathepsins B, C and D were determined in both supernatant and particulate fractions of two bovine muscles and rat liver by the use of synthetic or natural substrates. Comparison of the activities in bovine muscle with those in rat liver showed that total cathepsin B activity in skeletal muscle was approximately 52% of the activity obtained in rat liver whereas cathepsins C and D activities were approximately 2 and 25%, respectively.