Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1985 Jan 15;225(2):549–552. doi: 10.1042/bj2250549

Comparison of the structure of two cardiac troponin T isoforms.

V V Risnik, A D Verin, N B Gusev
PMCID: PMC1144623  PMID: 3977845

Abstract

Two isoforms of troponin T have been isolated from bovine cardiac muscle. One isoform has an Mr of 31000 and a pI at about 7.1, the corresponding values for the second isoform being 33000 and 6.5. Both isoforms have identical C- and N-terminal sequences, and, according to the data from tryptic-peptide mapping, a similar structure of the central and C-terminal domains. The large N-terminal peptides of troponin T isoforms differ in the content of glutamine/glutamic acid and alanine. It is concluded that the isoform with Mr 33000 has an additional peptide enriched with glutamic acid and alanine that is inserted between the N-terminal pentapeptide and the cysteine located 40-60 residues from the N-terminus.

Full text

PDF
549

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Clarke F. M., Lovell S. J., Masters C. J., Winzor D. J. Beef muscle troponin: evidence for multiple forms of troponin-T. Biochim Biophys Acta. 1976 Apr 14;427(2):617–626. doi: 10.1016/0005-2795(76)90205-1. [DOI] [PubMed] [Google Scholar]
  2. Dhoot G. K., Frearson N., Perry S. V. Polymorphic forms of troponin T and troponin C and their localization in striated muscle cell types. Exp Cell Res. 1979 Sep;122(2):339–350. doi: 10.1016/0014-4827(79)90310-0. [DOI] [PubMed] [Google Scholar]
  3. Dhoot G. K., Gell P. G., Perry S. V. The localization of the different forms of troponin I in skeletal and cardiac muscle cells. Exp Cell Res. 1978 Dec;117(2):357–370. doi: 10.1016/0014-4827(78)90149-0. [DOI] [PubMed] [Google Scholar]
  4. Gusev N. B., Barskaya N. V., Verin A. D., Duzhenkova I. V., Khuchua Z. A., Zheltova A. O. Some properties of cardiac troponin T structure. Biochem J. 1983 Jul 1;213(1):123–129. doi: 10.1042/bj2130123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Heywood S. M., Thibault M. C., Siegel E. Control of gene expression in muscle development. Cell Muscle Motil. 1983;3:157–193. doi: 10.1007/978-1-4615-9296-9_6. [DOI] [PubMed] [Google Scholar]
  6. Hirabayashi T. Two-dimensional gel electrophoresis of chicken skeletal muscle proteins with agarose gels in the first dimension. Anal Biochem. 1981 Nov 1;117(2):443–451. doi: 10.1016/0003-2697(81)90804-6. [DOI] [PubMed] [Google Scholar]
  7. Jacobson G. R., Schaffer M. H., Stark G. R., Vanaman T. C. Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystine residues. J Biol Chem. 1973 Oct 10;248(19):6583–6591. [PubMed] [Google Scholar]
  8. Moir A. J., Cole H. A., Perry S. V. The phosphorylation sites of troponin T from white skeletal muscle and the effects of interaction with troponin C on their phosphorylation by phosphorylase kinase. Biochem J. 1977 Feb 1;161(2):371–382. doi: 10.1042/bj1610371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Murakami U., Uchida K. Two-dimensional electrophoresis of troponin complex with nonequilibrium pH gradient-sodium dodecyl sulfate polyacrylamide slab gel. J Biochem. 1984 Jun;95(6):1577–1584. doi: 10.1093/oxfordjournals.jbchem.a134770. [DOI] [PubMed] [Google Scholar]
  10. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  11. Obinata T., Takano-Ohmuro H., Matsuda R. Changes in troponin-T and myosin isozymes during development of normal and dystrophic chicken muscles. FEBS Lett. 1980 Nov 3;120(2):195–198. doi: 10.1016/0014-5793(80)80296-1. [DOI] [PubMed] [Google Scholar]
  12. Pearlstone J. R., Carpenter M. R., Johnson P., Smillie L. B. Amino-acid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1902–1906. doi: 10.1073/pnas.73.6.1902. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Putney S. D., Herlihy W. C., Schimmel P. A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing. Nature. 1983 Apr 21;302(5910):718–721. doi: 10.1038/302718a0. [DOI] [PubMed] [Google Scholar]
  14. REISFELD R. A., LEWIS U. J., WILLIAMS D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature. 1962 Jul 21;195:281–283. doi: 10.1038/195281a0. [DOI] [PubMed] [Google Scholar]
  15. Wilkinson J. M., Grand R. J. Comparison of amino acid sequence of troponin I from different striated muscles. Nature. 1978 Jan 5;271(5640):31–35. doi: 10.1038/271031a0. [DOI] [PubMed] [Google Scholar]
  16. Wilkinson J. M., Moir A. J., Waterfield M. D. The expression of multiple forms of troponin T in chicken-fast-skeletal muscle may result from differential splicing of a single gene. Eur J Biochem. 1984 Aug 15;143(1):47–56. doi: 10.1111/j.1432-1033.1984.tb08337.x. [DOI] [PubMed] [Google Scholar]
  17. Wilkinson J. M. The components of troponin from chicken fast skeletal muscle. A comparison of troponin T and troponin I from breast and leg muscle. Biochem J. 1978 Jan 1;169(1):229–238. doi: 10.1042/bj1690229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wilkinson J. M. The preparation and properties of the components of troponin B. Biochim Biophys Acta. 1974 Aug 8;359(2):379–388. doi: 10.1016/0005-2795(74)90238-4. [DOI] [PubMed] [Google Scholar]
  19. Wilkinson J. M. Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur J Biochem. 1980 Jan;103(1):179–188. doi: 10.1111/j.1432-1033.1980.tb04302.x. [DOI] [PubMed] [Google Scholar]
  20. van Eerd J. P., Takahshi K. Determination of the complete amino acid sequence of bovine cardiac troponin C. Biochemistry. 1976 Mar 9;15(5):1171–1180. doi: 10.1021/bi00650a033. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES