Literature DB >> 7358047

Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene.

J M Wilkinson.   

Abstract

Troponin C has been isolated from rabbit slow skeletal and cardiac muscle and the complete amino acid sequence of the slow muscle protein determined. Amino acid analysis and peptide mapping of the cardiac protein showed it to be very similar to, if not identical with, the slow muscle protein. This identity has been proved by the isolation and characterisation of tryptic peptides from the cardiac protein. It seems very likely that troponin C from these two tissues is the product of a single gene, in contrast to troponin I and troponin T which are the products of different genes. The amino acid sequences shows only one difference from that of bovine cardiac troponin C, the highly conservative replacement of an aspartic for a glutamic acid at position 115. No differences were found in the N-terminal region where these proteins appear to have a lost one of the Ca2+ binding sites found in fast skeletal muscle troponin C. The possible significance of this finding in relation to the binding of troponin C to the different types of troponin I is discussed.

Entities:  

Mesh:

Substances:

Year:  1980        PMID: 7358047     DOI: 10.1111/j.1432-1033.1980.tb04302.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  25 in total

1.  Slow troponin T mRNA in striated muscles is expressed in both cell type and developmental stage specific manner.

Authors:  K Krishan; M J Morgan; W Zhao; G K Dhoot
Journal:  J Muscle Res Cell Motil       Date:  2000       Impact factor: 2.698

Review 2.  Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons.

Authors:  J H Collins
Journal:  J Muscle Res Cell Motil       Date:  1991-02       Impact factor: 2.698

3.  Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences.

Authors:  N D Moncrief; R H Kretsinger; M Goodman
Journal:  J Mol Evol       Date:  1990-06       Impact factor: 2.395

4.  Transient expression of fast troponin C transcripts in embryonic quail heart.

Authors:  A Stoutamyer; G K Dhoot
Journal:  J Muscle Res Cell Motil       Date:  2005-11-09       Impact factor: 2.698

5.  Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardium.

Authors:  W O Hancock; D A Martyn; L L Huntsman; A M Gordon
Journal:  Biophys J       Date:  1996-06       Impact factor: 4.033

6.  The nontranscribed chicken calmodulin pseudogene cross-hybridizes with mRNA from the slow-muscle troponin C gene.

Authors:  J A Putkey; S L Carroll; A R Means
Journal:  Mol Cell Biol       Date:  1987-04       Impact factor: 4.272

7.  Expression of the troponin complex genes: transcriptional coactivation during myoblast differentiation and independent control in heart and skeletal muscles.

Authors:  E A Bucher; P C Maisonpierre; S F Konieczny; C P Emerson
Journal:  Mol Cell Biol       Date:  1988-10       Impact factor: 4.272

8.  Stabilization of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains.

Authors:  M Sundaralingam; W Drendel; M Greaser
Journal:  Proc Natl Acad Sci U S A       Date:  1985-12       Impact factor: 11.205

9.  Comparison of the structure of two cardiac troponin T isoforms.

Authors:  V V Risnik; A D Verin; N B Gusev
Journal:  Biochem J       Date:  1985-01-15       Impact factor: 3.857

10.  Distribution of polymorphic forms of troponin components in extra- and intrafusal fibers of an avian slow muscle.

Authors:  M Miyazaki; N Toyota; Y Shimada
Journal:  Cell Tissue Res       Date:  1984       Impact factor: 5.249

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.