The Effect of Limited Proteolysis on Rabbit Muscle Creatine Kinase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1981 Oct 1

PMID 7039617

Citations 6

Authors

N C Price

S Murray

Affiliations

Soon will be listed here.

Abstract

Creatine kinase from rabbit muscle is inactivated by limited proteolysis with proteinase K from Tritirachium album. Gel-filtration and cross-linking studies showed that the limited proteolysis did not affect the molecular weight of the enzyme under non-denaturing conditions, but did cause changes in the reactivity of the reactive thiol group on each subunit and in the ability of the enzyme to form a 'transition-state analogue' complex in the presence of magnesium acetate plus ADP plus creatinine plus NaNO3.

Citing Articles

Hydrogen/deuterium exchange studies of native rabbit MM-CK dynamics.

Mazon H, Marcillat O, Forest E, Vial C Protein Sci. 2004; 13(2):476-86.

PMID: 14739330 PMC: 2286700. DOI: 10.1110/ps.03380604.

Mitochondrial creatine kinase binding to liposomes and vesicle aggregation: effect of cleavage by proteinase K.

Granjon T, Vial C, Buchet R, Vacheron M J Protein Chem. 2002; 20(8):593-9.

PMID: 11890199 DOI: 10.1023/a:1013763716762.

Proteinase K processing of rabbit muscle creatine kinase.

Leydier C, Andersen J, Couthon F, Forest E, Marcillat O, Denoroy L J Protein Chem. 1997; 16(1):67-74.

PMID: 9055209 DOI: 10.1023/a:1026347129083.

The refolding of denatured rabbit muscle creatine kinase. Search for intermediates in the refolding process and effect of modification at the reactive thiol group on refolding.

Price N, Stevens E Biochem J. 1982; 201(1):171-7.

PMID: 6805463 PMC: 1163623. DOI: 10.1042/bj2010171.

Monoclonal-antibody studies of creatine kinase. The proteinase K-cleavage site.

Morris G, FROST L, Head L Biochem J. 1985; 228(2):375-81.

PMID: 3893421 PMC: 1144995. DOI: 10.1042/bj2280375.

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