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PMID: 4029494 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

N-terminal sequence of creatine kinase from skeletal muscle of rabbit and rhesus monkey.

The International journal of biochemistry ·Vol. 17 ·No. 6 ·1985-00-00 ·Pages 749-52

Chegwidden WR, Hewett-Emmett D, Penny GG

Abstract

The first 20 amino acids from the N-terminus of skeletal muscle (MM) creatine kinase from both rabbit and rhesus monkey have been identified and these sequences show considerable homology. Contrary to an earlier report, the N-terminus was not found to be blocked. Both of these sequences show much less homology with the N-terminal sequence of heart muscle (MM) creatine kinase and no homology with that of the heart muscle mitochondrial (MiMi) isozyme. No homology was found between the N-terminal sequence of the mitochondrial isozyme and the URF (unidentified reading frame) proteins of the human mitochondrial genome, indicating that the mitochondrial enzyme is encoded by nuclear genes. This suggests the possibility that an N-terminal peptide may be cleaved from the mitochondrial isozyme on its translocation across the mitochondrial membrane.

MeSH Terms
Amino Acid Sequence Animals Creatine Kinase/isolation & purification Humans Isoenzymes Macaca mulatta Muscles/enzymology Rabbits Species Specificity
Chemicals
Isoenzymes Creatine Kinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Chegwidden W R
Hewett-Emmett D
Penny G G
Article Info
Journal
The International journal of biochemistry
Abbr.
Int J Biochem
ISSN
0020-711X
Published
1985-00-00
Pages
749-52
Language
English
Region
England
NLM ID
0250365
Subset
IM
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