Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1966 Sep;56(3):966–973. doi: 10.1073/pnas.56.3.966

Subunit structure of myosin, II. Heavy and light alkali components.

L C Gershman, P Dreizen, A Stracher
PMCID: PMC219954  PMID: 5230191

Full text

PDF
969

Images in this article

967Image
on p.967
967Image
on p.967
967Image
on p.967
970Image
on p.970
971Image
on p.971
971Image
on p.971
971Image
on p.971
972Image
on p.972

Selected References

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

  1. Dreizen P., Hartshorne D. J., Stracher A. The subunit structure of myosin. I. Polydispersity in 5 M guanidine. J Biol Chem. 1966 Jan 25;241(2):443–448. [PubMed] [Google Scholar]
  2. KAY C. M. The partial specific volume of muscle proteins. Biochim Biophys Acta. 1960 Mar 11;38:420–427. doi: 10.1016/0006-3002(60)91277-4. [DOI] [PubMed] [Google Scholar]
  3. KIELLEY W. W., HARRINGTON W. F. A model for the myosin molecule. Biochim Biophys Acta. 1960 Jul 15;41:401–421. doi: 10.1016/0006-3002(60)90037-8. [DOI] [PubMed] [Google Scholar]
  4. KOMINZ D. R., HOUGH A., SYMONDS P., LAKI K. The amino acid composition of action, myosin, tropomyosin and the meromyosins. Arch Biochem Biophys. 1954 May;50(1):148–159. doi: 10.1016/0003-9861(54)90017-x. [DOI] [PubMed] [Google Scholar]
  5. LOWEY S., COHEN C. Studies on the structure of myosin. J Mol Biol. 1962 Apr;4:293–308. doi: 10.1016/s0022-2836(62)80007-2. [DOI] [PubMed] [Google Scholar]
  6. LOWEY S., HOLTZER A. The homogeneity and molecular weights of the meromyosins and their relative proportions in myosin. Biochim Biophys Acta. 1959 Aug;34:470–484. doi: 10.1016/0006-3002(59)90300-2. [DOI] [PubMed] [Google Scholar]
  7. MUELLER H. MOLECULAR WEIGHT OF MYOSIN AND MEROMYOSINS BY ARCHIBALD EXPERIMENTS PERFORMED WITH INCREASING SPEED OF ROTATIONS. J Biol Chem. 1964 Mar;239:797–804. [PubMed] [Google Scholar]
  8. Mueller H. Characterization of the molecular region containing the active sites of myosin. J Biol Chem. 1965 Oct;240(10):3816–3828. [PubMed] [Google Scholar]
  9. RICE R. V. Conformation of individual macromolecular particles from myosin solution. Biochim Biophys Acta. 1961 Sep 30;52:602–604. doi: 10.1016/0006-3002(61)90427-9. [DOI] [PubMed] [Google Scholar]
  10. STRACHER A., CHAN P. C. Effect of p-chloromercuribenzoate on myosin A-adenosinetriphosphatase activity. Arch Biochem Biophys. 1961 Dec;95:435–440. doi: 10.1016/0003-9861(61)90173-4. [DOI] [PubMed] [Google Scholar]
  11. SZENT-GYORGYI A. G., BORBIRO M. Depolymerization of light meromyosin by urea. Arch Biochem Biophys. 1956 Jan;60(1):180–197. doi: 10.1016/0003-9861(56)90410-6. [DOI] [PubMed] [Google Scholar]
  12. TSAO T. C. Fragmentation of the myosin molecule. Biochim Biophys Acta. 1953 Jul;11(3):368–382. doi: 10.1016/0006-3002(53)90056-0. [DOI] [PubMed] [Google Scholar]
  13. Tonomura Y., Appel P., Morales M. On the molecular weight of myosin. II. Biochemistry. 1966 Feb;5(2):515–521. doi: 10.1021/bi00866a017. [DOI] [PubMed] [Google Scholar]
  14. WETLAUFER D. B., EDSALL J. T. Sedimentation of myosin in urea solutions. Biochim Biophys Acta. 1960 Sep 9;43:132–134. doi: 10.1016/0006-3002(60)90417-0. [DOI] [PubMed] [Google Scholar]
  15. WOODS E. F., HIMMELFARB S., HARRINGTON W. F. Studies on the structure of myosin in solution. J Biol Chem. 1963 Jul;238:2374–2385. [PubMed] [Google Scholar]
  16. YOUNG D. M., HIMMELFARB S., HARRINGTON W. F. ON THE STRUCTURAL ASSEMBLY OF THE POLYPEPTIDE CHAINS OF HEAVY MEROMYOSIN. J Biol Chem. 1965 Jun;240:2428–2436. [PubMed] [Google Scholar]
  17. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES