Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1981 May 1;195(2):463–469. doi: 10.1042/bj1950463

C-protein from rabbit soleus (red) muscle.

J E Callaway, P J Bechtel
PMCID: PMC1162910  PMID: 6797400

Abstract

A new form of skeletal-muscle C-protein has been isolated from rabbit soleus (red) muscle. This new form of C-protein has been purified to homogeneity by a procedure similar to that used to purify C-protein from white skeletal muscle. In soleus muscle, only this new form of C-protein could be detected, whereas in psoas (white) muscle, only the previously identified form of C-protein was detected. The content of C-protein in rabbit soleus muscle is comparable with that found in psoas muscle. Other rabbit skeletal muscles composed of a mixture of fibre types contained at least two forms of C-protein. C-Protein derived from red skeletal muscle bound to myosin isolated from either red or white tissue, with maximum binding occurring at a ratio of approximately 13 microgram of red C-protein/100 microgram of myosin. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate indicated that C-protein isolated from red skeletal muscle has a molecular weight approx. 7% greater than that of C-protein isolated from white skeletal muscle. The amino acid content of both forms of C-protein was similar but major differences in the mol % of isoleucine and threonine were found. Antiserum against C-protein from white rabbit skeletal muscle formed a single precipitin line with rabbit C-protein on double in agar. This antiserum did not form a precipitin line when diffused against red C-protein from rabbit skeletal muscle. Also, this antiserum bound specifically to the A-band region of myofibrils isolated from psoas (white) muscle, but it did not bind to myofibrils prepared from soleus (red) muscle.

Full text

PDF
463

Images in this article

466Fig. 2.
on p.466
467Fig. 4.
on p.467
468Fig. 5.
on p.468

Selected References

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

  1. Bechtel P. J. Identification of a high molecular weight actin-binding protein in skeletal muscle. J Biol Chem. 1979 Mar 25;254(6):1755–1758. [PubMed] [Google Scholar]
  2. Craig R., Offer G. The location of C-protein in rabbit skeletal muscle. Proc R Soc Lond B Biol Sci. 1976 Mar 16;192(1109):451–461. doi: 10.1098/rspb.1976.0023. [DOI] [PubMed] [Google Scholar]
  3. Gauthier G. F., Lowey S. Distribution of myosin isoenzymes among skeletal muscle fiber types. J Cell Biol. 1979 Apr;81(1):10–25. doi: 10.1083/jcb.81.1.10. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Head J. F., Weeks R. A., Perry S. V. Affinity-chromatographic isolation and some properties of troponin C from different muscle types. Biochem J. 1977 Mar 1;161(3):465–471. doi: 10.1042/bj1610465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Koretz J. F. Effects of C-protein on synthetic myosin filament structure. Biophys J. 1979 Sep;27(3):433–446. doi: 10.1016/S0006-3495(79)85227-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Moos C., Mason C. M., Besterman J. M., Feng I. N., Dubin J. H. The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J Mol Biol. 1978 Oct 5;124(4):571–586. doi: 10.1016/0022-2836(78)90172-9. [DOI] [PubMed] [Google Scholar]
  8. Moos C., Offer G., Starr R., Bennett P. Interaction of C-protein with myosin, myosin rod and light meromyosin. J Mol Biol. 1975 Sep 5;97(1):1–9. doi: 10.1016/s0022-2836(75)80017-9. [DOI] [PubMed] [Google Scholar]
  9. Offer G., Moos C., Starr R. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J Mol Biol. 1973 Mar 15;74(4):653–676. doi: 10.1016/0022-2836(73)90055-7. [DOI] [PubMed] [Google Scholar]
  10. Offer G. The antigenicity of myosin and C-protein. Proc R Soc Lond B Biol Sci. 1976 Mar 16;192(1109):439–449. doi: 10.1098/rspb.1976.0022. [DOI] [PubMed] [Google Scholar]
  11. Pepe F. A., Drucker B. The myosin filament. III. C-protein. J Mol Biol. 1975 Dec 25;99(4):609–617. doi: 10.1016/s0022-2836(75)80175-6. [DOI] [PubMed] [Google Scholar]
  12. Peter J. B., Barnard R. J., Edgerton V. R., Gillespie C. A., Stempel K. E. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry. 1972 Jul 4;11(14):2627–2633. doi: 10.1021/bi00764a013. [DOI] [PubMed] [Google Scholar]
  13. Seidel J. C. Studies on myosin from red and white skeletal muscles of the rabbit. II. Inactivation of myosin from red muscles under mild alkaline conditions. J Biol Chem. 1967 Dec 10;242(23):5623–5629. [PubMed] [Google Scholar]
  14. Starr R., Offer G. Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett. 1971 Jun 2;15(1):40–44. doi: 10.1016/0014-5793(71)80075-3. [DOI] [PubMed] [Google Scholar]
  15. Starr R., Offer G. The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem J. 1978 Jun 1;171(3):813–816. doi: 10.1042/bj1710813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Studier F. W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol. 1973 Sep 15;79(2):237–248. doi: 10.1016/0022-2836(73)90003-x. [DOI] [PubMed] [Google Scholar]
  17. Suzuki A., Goll D. E., Stromer M. H., Temple J. -actinin from red and white porcine muscle. Biochim Biophys Acta. 1973 Jan 25;295(1):188–207. doi: 10.1016/0005-2795(73)90087-1. [DOI] [PubMed] [Google Scholar]
  18. Wachsberger P. R., Pepe F. A. Purification of uterine myosin and synthetic filament formation. J Mol Biol. 1974 Sep 15;88(2):385–391. doi: 10.1016/0022-2836(74)90489-6. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Weeds A. G., Hall R., Spurway N. C. Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle. FEBS Lett. 1975 Jan 1;49(3):320–324. doi: 10.1016/0014-5793(75)80776-9. [DOI] [PubMed] [Google Scholar]
  21. 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]

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

RESOURCES