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Hydrolytic Enzymes in Bovine Skeletal Muscle. II. Proteolytic Activity of the Water‐Soluble Proteins Separated by Starch Gel Electrophoresis.
Author(s) -
RANDALL C. J.,
MacRAE H. F.
Publication year - 1967
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.1365-2621.1967.tb01288.x
Subject(s) - hydrolysis , chemistry , cathepsin , biochemistry , starch , proteolytic enzymes , substrate (aquarium) , leucine , enzyme , electrophoresis , cathepsin d , aminopeptidase , chromatography , skeletal muscle , biology , amino acid , anatomy , ecology
SUMMARY— Proteolytic activity of the water‐soluble proteins of bovine skeletal muscle separated in starch gels, was examined by the use of various synthetic and natural substrates, and by the use of inhibitors. A total of 10 electrophoretically‐separated bands hydrolyzed acetylphenylalanine‐β‐napthyl ester. Seven of the separated protein bands hydrolyzed four different substrates indicating the presence of more than one type of enzyme in each of the bands. Based on substrate hydrolysis, effects of inhibitors and heat stability, proteolytic activities resembling that of cathepsin 8, cathepsin C and leucine aminopeptidase were presumed to be present.