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PMID: 2973419 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

An example of substrate channeling between co-immobilized enzymes. Coupled activity of myosin ATPase and creatine kinase bound to frog heart myofilaments.

FEBS letters ·Vol. 240 ·No. 1-2 ·1988-11-21 ·Pages 181-5

Arrio-Dupont M

Abstract

In myofilaments obtained by Triton X-100 lysis of frog heart cells in high ionic strength medium, the activity of bound creatine kinase cannot be detected by a coupled enzymatic assay. ATP is channelized toward myosin ATPase, through the unstirred layer near myofilaments and cannot diffuse into the bulk solution. Model systems based upon the coupled kinetics of enzymes co-immobilized on the same surface may explain this behaviour. This may also account for why myofilament-bound creatine kinase is more efficient than free enzyme in the cytosol for the physiological recycling of ADP into ATP.

MeSH Terms
Actin Cytoskeleton/enzymology Adenosine Triphosphate/metabolism Animals Anura Creatine Kinase/metabolism Diffusion Enzymes, Immobilized Kinetics Myocardium/enzymology Myosins/metabolism Osmolar Concentration
Chemicals
Enzymes, Immobilized Adenosine Triphosphate Creatine Kinase Myosins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Arrio-Dupont M
INSERM U-241, Université Paris Sud, Orsay, France.
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1988-11-21
Pages
181-5
Language
English
Region
England
NLM ID
0155157
Subset
IM
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