Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1977 Mar 1;161(3):465–471. doi: 10.1042/bj1610465

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

J F Head, R A Weeks, S V Perry
PMCID: PMC1164530  PMID: 851428

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.

Full text

PDF
468-2

Images in this article

468-2PLATE 2
on p.468-2
468-1PLATE 1
on p.468-1

Selected References

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

  1. Brekke C. J., Greaser M. L. Separation and characterization of the troponin components from bovine cardiac muscle. J Biol Chem. 1976 Feb 10;251(3):866–871. [PubMed] [Google Scholar]
  2. Bremel R. D. Myosin linked calcium regulation in vertebrate smooth muscle. Nature. 1974 Nov 29;252(5482):405–407. doi: 10.1038/252405a0. [DOI] [PubMed] [Google Scholar]
  3. Cole H. A., Perry S. V. The phosphorylation of troponin I from cardiac muscle. Biochem J. 1975 Sep;149(3):525–533. doi: 10.1042/bj1490525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Collins J. H. Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequences. Biochem Biophys Res Commun. 1974 May 7;58(1):301–308. doi: 10.1016/0006-291x(74)90927-9. [DOI] [PubMed] [Google Scholar]
  5. Cuatrecasas P., Wilchek M., Anfinsen C. B. Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci U S A. 1968 Oct;61(2):636–643. doi: 10.1073/pnas.61.2.636. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cummins P., Perry S. V. Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscle. Biochem J. 1974 Jul;141(1):43–49. doi: 10.1042/bj1410043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cummins P., Perry S. V. The subunits and biological activity of polymorphic forms of tropomyosin. Biochem J. 1973 Aug;133(4):765–777. doi: 10.1042/bj1330765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ebashi S., Toyo-Oka T., Nonmura Y. Gizzard Troponin. J Biochem. 1975 Oct;78(4):859–861. doi: 10.1093/oxfordjournals.jbchem.a130976. [DOI] [PubMed] [Google Scholar]
  9. Ebashi S., Wakabayashi T., Ebashi F. Troponin and its components. J Biochem. 1971 Feb;69(2):441–445. doi: 10.1093/oxfordjournals.jbchem.a129486. [DOI] [PubMed] [Google Scholar]
  10. Head J. F., Perry S. V. The interaction of the calcium-binding protein (troponin C) with bivalent cations and the inhibitory protein (troponin I). Biochem J. 1974 Feb;137(2):145–154. doi: 10.1042/bj1370145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hirabayashi T., Perry S. V. An immunochemical study of the calcium ion-binding protein (troponin-C) and the inhibitory protein (troponin-I) of the troponin complex and their interaction. Biochim Biophys Acta. 1974 Jun 7;351(2):273–289. doi: 10.1016/0005-2795(74)90189-5. [DOI] [PubMed] [Google Scholar]
  12. Hitchcock S. E. Regulation of muscle contraction. Effect of calcium on the affinity of troponin for actin and tropomyosin. Biochemistry. 1973 Jun 19;12(13):2509–2513. doi: 10.1021/bi00737a022. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. March S. C., Parikh I., Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem. 1974 Jul;60(1):149–152. doi: 10.1016/0003-2697(74)90139-0. [DOI] [PubMed] [Google Scholar]
  15. Perry S. V., Cole H. A. Phosphorylation of troponin and the effects of interactions between the components of the complex. Biochem J. 1974 Sep;141(3):733–743. doi: 10.1042/bj1410733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. STEERS E., Jr, CRAVEN G. R., ANFINSEN C. B., BETHUNE J. L. EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2478–2484. [PubMed] [Google Scholar]
  17. Syska H., Perry S. V., Trayer I. P. A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle. FEBS Lett. 1974 Apr 1;40(2):253–257. doi: 10.1016/0014-5793(74)80238-3. [DOI] [PubMed] [Google Scholar]
  18. Syska H., Wilkinson J. M., Grand R. J., Perry S. V. The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem J. 1976 Feb 1;153(2):375–387. doi: 10.1042/bj1530375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tsukui R., Ebashi S. Cardiac troponin. J Biochem. 1973 May;73(5):1119–1121. doi: 10.1093/oxfordjournals.jbchem.a130168. [DOI] [PubMed] [Google Scholar]
  20. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  21. Wilkinson J. M., Perry S. V., Cole H. A., Trayer I. P. The regulatory proteins of the myofibril. Separation and biological activity of the components of inhibitory-factor preparations. Biochem J. 1972 Mar;127(1):215–228. doi: 10.1042/bj1270215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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]
  23. van Eerd J. P., Takahashi K. The amino acid sequence of bovine cardiac tamponin-C. Comparison with rabbit skeletal troponin-C. Biochem Biophys Res Commun. 1975 May 5;64(1):122–127. doi: 10.1016/0006-291x(75)90227-2. [DOI] [PubMed] [Google Scholar]

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

RESOURCES