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Activities of cathepsins A and D in cod muscle
Author(s) -
McLay R.
Publication year - 1980
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740311012
Subject(s) - cathepsin , biochemistry , chemistry , hydrolysis , cathepsin o , substrate (aquarium) , cathepsin l , cathepsin b , cathepsin d , cathepsin a , substrate specificity , cathepsin s , enzyme , biology , ecology
Cathepsin A has been demonstrated in cod muscle. Cathepsins A and D were partially separated and purified from cod muscle. Cathepsin A and D are essentially similar to those from other sources. Cathepsin A acts optimally on the synthetic substrate CBZ‐α‐L‐glutamyl‐L‐tyrosine at pH 5.0, whereas cathepsin D hydrolyses haemoglobin optimally at pH 3.8. Cathepsin D did not hydrolyse the synthetic peptides acted upon by cathepsins A, B or C.