Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 May 1;171(2):413–418. doi: 10.1042/bj1710413

Troponin-like proteins from muscles of the scallop, Aequipecten irradians.

A Goldberg, W Lehman
PMCID: PMC1183970  PMID: 148888

Abstract

Ca2+ regulation of molluscan actomyosin adenosine triphosphatase is known to be associated with the myosin molecule. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, however, also suggests the possible presence of troponin, a thin-filament-linked Ca2+-regulatory complex. In the present study, scallop troponin and tropomyosin were prepared and complexed with rabbit actin; the resulting synthetic thin filaments form a Ca2+-dependent actomyosin adenosine triphosphatase with Ca2+-insensitive rabbit myosin, indicating that the troponin in scallops is potentially functional. Scallop troponin I was isolated and mixed with chicken troponin C and troponin T, forming a functional hybrid troponin complex, indicating that scallop and vertebrate troponins may act by a common mechanism. Densitometry of sodium dodecyl sulphate/polyacrylamide gels reveals that in synthetic thin filaments there are larger amounts of troponin than are present in native thin filaments. Amounts present in the intact muscle were not determined.

Full text

PDF
413

Images in this article

416-1PLATE 1
on p.416-1

Selected References

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

  1. Eaton B. L., Kominz D. R., Eisenberg E. Correlation between the inhibition of the acto-heavy meromyosin ATPase and the binding of tropomyosin to F-actin: effects of Mg2+, KCl, troponin I, and troponin C. Biochemistry. 1975 Jun 17;14(12):2718–2725. doi: 10.1021/bi00683a025. [DOI] [PubMed] [Google Scholar]
  2. Greaser M. L., Gergely J. Reconstitution of troponin activity from three protein components. J Biol Chem. 1971 Jul 10;246(13):4226–4233. [PubMed] [Google Scholar]
  3. Hartshorne D. J., Mueller H. Fractionation of troponin into two distinct proteins. Biochem Biophys Res Commun. 1968 Jun 10;31(5):647–653. doi: 10.1016/0006-291x(68)90610-4. [DOI] [PubMed] [Google Scholar]
  4. Hartshorne D. J., Mueller H. The preparation of tropomyosin and troponin from natural actomyosin. Biochim Biophys Acta. 1969 Mar;175(2):301–319. doi: 10.1016/0005-2795(69)90008-7. [DOI] [PubMed] [Google Scholar]
  5. Haselgrove J. C. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J Mol Biol. 1975 Feb 15;92(1):113–143. doi: 10.1016/0022-2836(75)90094-7. [DOI] [PubMed] [Google Scholar]
  6. Kendrick-Jones J., Lehman W., Szent-Györgyi A. G. Regulation in molluscan muscles. J Mol Biol. 1970 Dec 14;54(2):313–326. doi: 10.1016/0022-2836(70)90432-8. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Lehman W., Bullard B., Hammond K. Calcium-dependent myosin from insect flight muscles. J Gen Physiol. 1974 May;63(5):553–563. doi: 10.1085/jgp.63.5.553. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lehman W. Calcium ion-dependent myosin from decapod-crustacean muscles. Biochem J. 1977 May 1;163(2):291–296. doi: 10.1042/bj1630291. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lehman W., Regenstein J. M., Ransom A. L. The stoichiometry of the components of arthropod thin filaments. Biochim Biophys Acta. 1976 May 20;434(1):215–222. doi: 10.1016/0005-2795(76)90053-2. [DOI] [PubMed] [Google Scholar]
  11. Lehman W., Szent-Györgyi A. G. Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J Gen Physiol. 1975 Jul;66(1):1–30. doi: 10.1085/jgp.66.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lehman W., Szent-Györgyi G. Activation of the adenosine triphosphatase of Limulus polyphemus actomyosin by tropomyosin. J Gen Physiol. 1972 Apr;59(4):375–387. doi: 10.1085/jgp.59.4.375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. MOMMAERTS W. F. H. M., PARRISH R. G. Studies on myosin. I. Preparation and criteria of purity. J Biol Chem. 1951 Feb;188(2):545–552. [PubMed] [Google Scholar]
  14. Morimoto K., Harrington W. F. Evidence for structural changes in vertebrate thick filaments induced by calcium. J Mol Biol. 1974 Sep 25;88(3):693–709. doi: 10.1016/0022-2836(74)90417-3. [DOI] [PubMed] [Google Scholar]
  15. Potter J. D. The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils. Arch Biochem Biophys. 1974 Jun;162(2):436–441. doi: 10.1016/0003-9861(74)90202-1. [DOI] [PubMed] [Google Scholar]
  16. Regenstein J. M., Szent-Gyäorgyi A. G. Regulatory proteins of lobster striated muscle. Biochemistry. 1975 Mar 11;14(5):917–925. doi: 10.1021/bi00676a007. [DOI] [PubMed] [Google Scholar]
  17. Szent-Györgyi A. G., Cohen C., Kendrick-Jones J. Paramyosin and the filaments of molluscan "catch" muscles. II. Native filaments: isolation and characterization. J Mol Biol. 1971 Mar 14;56(2):239–258. doi: 10.1016/0022-2836(71)90462-1. [DOI] [PubMed] [Google Scholar]
  18. 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]

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

RESOURCES