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PMID: 851428 Published · ppublish English Journal Article

Affinity-chromatographic isolation and some properties of troponin C from different muscle types.

The Biochemical journal ·Vol. 161 ·No. 3 ·1977-03-01 ·Pages 465-71

Head JF, Weeks RA, Perry SV

Abstract

1. The formation of a complex between troponin I and troponin C that is stable in 6M-urea and dependent on Ca2+ was demonstrated in extracts of vertebrate striated and smooth muscles. 2. A method using troponin I coupled to Sepharose is described for the rapid isolation of troponin C from striated and smooth muscles of vertebrates. 3. Troponin C of rabbit cardiac muscle differs significantly in amino acid composition from troponin C of skeletal muscle. The primary structures of troponin C of red and white skeletal muscle are very similar. 4. The troponin C-like protein isolated from rabbit uterus muscle has a slightly different amino acid composition, but possess many similar properties to the forms of troponin C isolated from other muscle types. 5. The electrophoretic mobilities of the I-troponin C complexes formed from components isolated from different muscle types are determined by the troponin I component.

MeSH Terms
Amino Acids/analysis Animals Chromatography, Affinity/methods Muscle Proteins/isolation & purification Muscle, Smooth/analysis Muscles/analysis Rabbits Troponin/analogs & derivatives,isolation & purification
Chemicals
Amino Acids Muscle Proteins Troponin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Head J F
Weeks R A
Perry S V
References (23)
23 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1610465
Published
1977-03-01
Pages
465-71
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1164530
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1610465 PMC Full Text View journal details
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