Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1966 Feb 1;28(2):375–389. doi: 10.1083/jcb.28.2.375

AN ELECTRON MICROSCOPE STUDY OF CANINE CARDIAC MYOSIN AND SOME OF ITS AGGREGATES

John A Carney 1, Arnold L Brown Jr 1
PMCID: PMC2106928  PMID: 5914697

Abstract

The morphology of the canine cardiac myosin molecule has been investigated in the electron microscope with Hall's mica-replica technique. The molecule is an elongated rod (shaft) of nonuniform diameter with a globular expansion (head) on one end. Statistical analysis of the lengths of 1908 molecules showed that the mean length was 1610 ± 250 A; the mean length of the head was 210 ± 20 A; and the diameter of the head and that of the shaft were 35 to 40 and 15 to 20 A, respectively. About one-third of the molecules had single or multiple, fairly sharp, angulations along their shafts. Rarely, some details of the substructure of the molecule have been observed. Large, spindle-shaped aggregates, measuring 0.5 to 1 µ in length and 50 to 100 A in diameter, were produced by dilution of the myosin solutions. These aggregates were readily visualized in the electron microscope by means of Huxley's negative-staining technique. Projections often were visible along the length of the aggregates except at a central zone where they were frequently absent. The aggregates resembled the thick myofilaments of the myocardium and appeared similar to those produced by Huxley from skeletal myosin solutions.

Full Text

The Full Text of this article is available as a PDF (1.4 MB).

Selected References

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

  1. BRAHMS J., KAY C. M. Molecular and enzymatic properties of cardiac myosin A as compared with those of skeletal myosin A. J Biol Chem. 1963 Jan;238:198–205. [PubMed] [Google Scholar]
  2. BRAHMS J., KAY C. M. Molecular and enzymatic studies of cardiac myosin. J Mol Biol. 1962 Jul;5:132–137. doi: 10.1016/s0022-2836(62)80068-0. [DOI] [PubMed] [Google Scholar]
  3. Bailey K. Myosin and adenosinetriphosphatase. Biochem J. 1942 Feb;36(1-2):121–139. doi: 10.1042/bj0360121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Carney J. A., Brown A. L., Jr Human cardiac myosin: electron microscopic observations. Circ Res. 1965 Oct;17(4):336–339. doi: 10.1161/01.res.17.4.336. [DOI] [PubMed] [Google Scholar]
  5. DAVIS J. O., CARROLL W. R., TRAPASSO M., YANKOPOULOS N. A. Chemical characterization of cardiac myosin from normal dogs and from dogs with chronic congestive heart failure. J Clin Invest. 1960 Sep;39:1463–1471. doi: 10.1172/JCI104165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. ELLENBOGEN E., IYENGAR R., STERN H., OLSON R. E. Characterization of myosin from normal dog heart. J Biol Chem. 1960 Sep;235:2642–2648. [PubMed] [Google Scholar]
  7. GELOTTE B. Myosin from cardiac muscle. Biochim Biophys Acta. 1951 Sep;7(3):378–386. doi: 10.1016/0006-3002(51)90041-8. [DOI] [PubMed] [Google Scholar]
  8. HALL C. E. Measurement of globular protein molecules by electron microscopy. J Biophys Biochem Cytol. 1960 Jul;7:613–618. doi: 10.1083/jcb.7.4.613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HUXLEY H. E. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. J Mol Biol. 1963 Sep;7:281–308. doi: 10.1016/s0022-2836(63)80008-x. [DOI] [PubMed] [Google Scholar]
  10. HUXLEY H. E. The double array of filaments in cross-striated muscle. J Biophys Biochem Cytol. 1957 Sep 25;3(5):631–648. doi: 10.1083/jcb.3.5.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. MUELLER H., FRANZEN J., RICE R. V., OLSON R. E. CHARACTERIZATION OF CARDIAC MYOSIN FROM THE DOG. J Biol Chem. 1964 May;239:1447–1456. [PubMed] [Google Scholar]
  13. MUELLER H., THEINER M., OLSON R. E. MACROMOLECULAR FRAGMENTS OF CANINE CARDIAC MYOSIN OBTAINED BY TRYPTIC DIGESTION. J Biol Chem. 1964 Jul;239:2153–2159. [PubMed] [Google Scholar]
  14. NODA H., EBASHI S. Aggregation of myosin A. Biochim Biophys Acta. 1960 Jul 15;41:386–392. doi: 10.1016/0006-3002(60)90035-4. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. SZENT-GYORGYI A. G., COHEN C. Role of proline in polypeptide chain configuration of proteins. Science. 1957 Oct 11;126(3276):697–698. doi: 10.1126/science.126.3276.697. [DOI] [PubMed] [Google Scholar]
  17. SZENT-GYORGYI A. G. Meromyosins, the subunits of myosin. Arch Biochem Biophys. 1953 Feb;42(2):305–320. doi: 10.1016/0003-9861(53)90360-9. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. ZOBEL C. R., CARLSON F. D. An electron microscopic investigation of myosin and some of its aggregates. J Mol Biol. 1963 Jul;7:78–89. doi: 10.1016/s0022-2836(63)80020-0. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES