Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1962 Dec 1;15(3):401–416. doi: 10.1083/jcb.15.3.401

FINE STRUCTURAL LOCALIZATION OF ADENOSINETRIPHOSPHATASE ACTIVITY IN HEART MUSCLE MYOFIBRILS

Lois W Tice 1, Russell J Barrnett 1
PMCID: PMC2106161  PMID: 13981351

Abstract

Activity of myofibrillar adenosinetriphosphatase was demonstrated histochemically at a fine structural level in isolated, unfixed or hydroxyadipaldehyde-fixed cardiac myofibrils in the rat, using a lead precipitation technique and either Ca++ or Mg++ as activating ion. Activity in relaxed myofibrils was found in the A band, but not the H, I, or Z bands. Deposits of final product frequently exhibited an axial periodicity of near 365 A, and bore a close relationship to filaments within the A band. Several patterns of distribution occurred in contracted myofibrils. In myofibrils which had shortened to the point of disappearance of the I band, final product was distributed throughout the sarcomere, except for the unreactive Z band. A second type of distribution occurred in strongly contracted fibers in which there was intensification of activity in the center of the sarcomere. These findings are discussed in the light of the recent morphological evidence and it is suggested that the distribution of final product is consistent with localization of enzyme activity to the cross-bridges between the thick and thin filaments.

Full Text

The Full Text of this article is available as a PDF (1.5 MB).

Selected References

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

  1. CAULFIELD J. B. Effects of varying the vehicle for OsO4 in tissue fixation. J Biophys Biochem Cytol. 1957 Sep 25;3(5):827–830. doi: 10.1083/jcb.3.5.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. FINCK H., HOLTZER H., MARSHALL J. M., Jr An immunochemical study of the distribution of myosin in glycerol extracted muscle. J Biophys Biochem Cytol. 1956 Jul 25;2(4 Suppl):175–178. doi: 10.1083/jcb.2.4.175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GERGELY J. The relaxing factor of muscle. Ann N Y Acad Sci. 1959 Aug 28;81:490–504. doi: 10.1111/j.1749-6632.1959.tb49330.x. [DOI] [PubMed] [Google Scholar]
  4. GILEV V. P. A study of myofibril sarcomere structure during contraction. J Cell Biol. 1962 Jan;12:135–147. doi: 10.1083/jcb.12.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HANSON J., HUXLEY H. E. Quantitative studies on the structure of cross-striated myofibrils. II. Investigations by biochemical techniques. Biochim Biophys Acta. 1957 Feb;23(2):250–260. doi: 10.1016/0006-3002(57)90326-8. [DOI] [PubMed] [Google Scholar]
  6. HOLTZER H., MARSHALL J. M., Jr, FINCK H. An analysis of myogenesis by the use of fluorescent antimyosin. J Biophys Biochem Cytol. 1957 Sep 25;3(5):705–724. doi: 10.1083/jcb.3.5.705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. HUXLEY H., HANSON J. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature. 1954 May 22;173(4412):973–976. doi: 10.1038/173973a0. [DOI] [PubMed] [Google Scholar]
  9. KARRER H. E. The striated musculature of blood vessels. I. General cell morphology. J Biophys Biochem Cytol. 1959 Dec;6:383–392. doi: 10.1083/jcb.6.3.383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. PADYKULA H. A., HERMAN E. The specificity of the histochemical method for adenosine triphosphatase. J Histochem Cytochem. 1955 May;3(3):170–195. doi: 10.1177/3.3.170. [DOI] [PubMed] [Google Scholar]
  12. PERRY S. V. Creatine phosphokinase and the enzymic and contractile properties of the isolated myofibril. Biochem J. 1954 Jul;57(3):427–434. doi: 10.1042/bj0570427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. PERRY S. V. The adenosinetriphosphatase activity of myofibrils isolated from skeletal muscle. Biochem J. 1951 Mar;48(3):257–265. doi: 10.1042/bj0480257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. SPIRO D. The ultrastructure of striated muscle at various sarcomere lengths. J Biophys Biochem Cytol. 1956 Jul 25;2(4 Suppl):157–162. doi: 10.1083/jcb.2.4.157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]

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

RESOURCES