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PMID: 978749 Published · ppublish English Journal Article

Human skeletal muscle proteins. The primary structure of troponin C.

Journal of molecular evolution ·Vol. 8 ·No. 3 ·1976-10-27 ·Pages 251-70

Romero-Herrera AE, Castillo O, Lehmann H

Abstract

The primary structure of the major component of human skeletal muscle troponin C has been established. The troponin C was purified by ammonium sulphate and isoelectric fractionation, followed by two chromatographic steps on DEAE Sephadex. The sequence was determined from the different overlapping enzymic peptides and by dansyl-Edman degradation. The only difference between rabbit skeletal muscle troponin C and the major component of human skeletal troponin C was found at position 112: Ala (rabbit), Pro (human). The partial amino acid sequence of the first 86 residues of the minor component of human skeletal troponin C was found to resemble the troponin C from bovine cardiac muscle. The only difference between them, has tentatively been located at position 62: Glu (human), Asp (bovine). These similarities suggest that troponin C is, from the point of view of molecular, one of the most conservative proteins so far studied.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Biological Evolution Humans Muscle Proteins/isolation & purification Muscles Peptide Fragments/analysis Subtilisins Thermolysin Troponin/isolation & purification Trypsin
Chemicals
Amino Acids Muscle Proteins Peptide Fragments Troponin Subtilisins Trypsin Thermolysin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Romero-Herrera A E
Castillo O
Lehmann H
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32 references, click to expand
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Article Info
Journal
Journal of molecular evolution
Abbr.
J Mol Evol
ISSN
0022-2844
DOI
10.1007/BF01730999
Published
1976-10-27
Pages
251-70
Language
English
Region
Germany
NLM ID
0360051
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01730999 View journal details
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