On the turnover and proteolysis of catalase in tissues of the guinea pig and acatalasemic mice

Jones G.L. and Masters C.J. (1976) On the turnover and proteolysis of catalase in tissues of the guinea pig and acatalasemic mice. Archives of Biochemistry and Biophysics, 173 2: 463-471. doi:10.1016/0003-9861(76)90283-6


Author Jones G.L.
Masters C.J.
Title On the turnover and proteolysis of catalase in tissues of the guinea pig and acatalasemic mice
Journal name Archives of Biochemistry and Biophysics   Check publisher's open access policy
ISSN 1096-0384
Publication date 1976-01-01
Sub-type Article (original research)
DOI 10.1016/0003-9861(76)90283-6
Volume 173
Issue 2
Start page 463
End page 471
Total pages 9
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract Turnover characteristics (half-lives and rate constants for synthesis and degradation) have been determined for the catalases of guinea pig and three different strains of mice by means of the kinetics of return of enzyme activity after inhibition with 3-amino-1,2,4-triazole. The catalase of hypocatalasemic mice (strain CsD) did not display an appreciably different half-life to that of the wild-type mice, but catalase in the tissues of acatalasemic mice (strain CsB) exhibited a half-life which was only half that of the wild type, while the half-life of guinea pig catalase was more than twice that of wild-type mice. Significant differences were also noticed in regard to the in vitro susceptibility of the catalases of these animals to protease inactivation. Large-granule (lysosomal, mitochondrial and peroxisomal) extracts proved far more susceptible to protease inactivation than cytosol extracts, and marked changes in the heteromorph pattern of mouse liver cytosol catalase were observed to accompany limited proteolysis. These results support the conclusion that the in vitro susceptibility of proteases may be an important determining factor in the rate of degradation of an enzyme in vivo.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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