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PMID: 1531959 Published · ppublish English Journal Article

The importance of C-terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I.

FEBS letters ·Vol. 297 ·No. 3 ·1992-02-10 ·Pages 237-40

Makuch R, Kołakowski J, Dabrowska R

Abstract

Proteolytic elimination of three C-terminal amino acid residues from actin weakens its interaction with caldesmon and troponin I and, in consequence, lowers the inhibitory effects of both proteins on actomyosin ATPase activity. These results prove the importance of C-terminal extremity of actin to the overall interaction of this protein with caldesmon and troponin I.

MeSH Terms
Actins/chemistry,physiology Animals Ca(2+) Mg(2+)-ATPase/metabolism Calmodulin-Binding Proteins/physiology Chickens Enzyme Activation Myosins/antagonists & inhibitors Troponin/physiology Troponin I
Chemicals
Actins Calmodulin-Binding Proteins Troponin Troponin I Ca(2+) Mg(2+)-ATPase Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Makuch R
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Kołakowski J
Dabrowska R
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1992-02-10
Pages
237-40
Language
English
Region
England
NLM ID
0155157
Subset
IM
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