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Retinol inhibition of some proteolytic enzymes
Author(s) -
Tappel A. L.,
Dillard C. J.
Publication year - 1968
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02531190
Subject(s) - biochemistry , proteolytic enzymes , chemistry , retinol , enzyme , cathepsin , pronase , cathepsin d , trypsin , vitamin
Automated analyses were used to determine the effect of retinol on the activity of the following proteolytic enzymes: ficin (EC 3.4.4.12), bromelain (EC 3.4.4. 24), trypsin (EC 3.4.4.4.), chymotrypsin A (EC 3.4.4.5), papain (EC 3.4.4.10), clostridiopeptidase A (EC 3.4.4.19), pepsin (EC 3.4.4.1), cathepsin D (EC 3.4.4. 23) from rat‐liver and rat‐kidney lysosomes and the nonspecific proteolytic enzyme, pronase. Of these proteolytic enzymes only ficin, bromelain, and rat‐kidney lysosomal cathepsin D were inhibited significantly by 1×10 −4 M retinol. Some nonproteolytic enzymes not inhibited by retinol were acid phosphatase (EC 3.1.3.2), β‐acetylglucosaminidase (EC 3.2.1.30), arylsulfatase (EC 3.1.6.1), and pyruvate kinase (EC 2.7.1.40). The inhibition of cathepsin D varied with the substrate used, being greater with hemoglobin than with ovalbumin or bovine serum albumin. Carotene and retinol inhibited ficin and cathepsin D to similar extents. Retinol inhibition of ficin was partially reversible. These studies of proteolytic enzyme inhibition by retinol serve as a simple model for studying retinol‐protein interactions in vitro.