Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1963 May;87(2):233–238. doi: 10.1042/bj0870233

The effect of actin on the magnesium-activated adenosine triphosphatase of heavy meromyosin

L Leadbeater 1,*, S V Perry 1
PMCID: PMC1201880  PMID: 13928816

Full text

PDF
233

Selected References

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

  1. ASHLEY C. A., ARASIMAVICIUS A., HASS G. M. Chemical studies of isolated myofibrils in vitro. I. The role of magnesium, calcium and nitrogen-phosphorus partition in contraction induced with adenosinetriphosphate. Exp Cell Res. 1956 Feb;10(1):1–13. doi: 10.1016/0014-4827(56)90064-7. [DOI] [PubMed] [Google Scholar]
  2. BARANY M., BARANY K. Studies on "active centers" of L-myosin. Biochim Biophys Acta. 1959 Oct;35:293–309. doi: 10.1016/0006-3002(59)90378-6. [DOI] [PubMed] [Google Scholar]
  3. BENDALL J. R. Further observations on a factor (The `Marsh' factor) effecting relaxation of ATP-shortened muscle-fibre models and the effect of Ca and Mg ions upon it. J Physiol. 1953 Aug;121(2):232–254. doi: 10.1113/jphysiol.1953.sp004944. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BLUM J. J., MORALES M. F. The interaction of myosin with adenosine triphosphate. Arch Biochem Biophys. 1953 Mar;43(1):208–230. doi: 10.1016/0003-9861(53)90100-3. [DOI] [PubMed] [Google Scholar]
  5. BOZLER E. Evidence of an ATP-actomyosin complex in relaxed muscle and its response to calcium ions. Am J Physiol. 1952 Mar;168(3):760–765. doi: 10.1152/ajplegacy.1952.168.3.760. [DOI] [PubMed] [Google Scholar]
  6. GERGELY J., GOUVEA M. A., KARIBIAN D. Fragmentation of myosin by chymotrypsin. J Biol Chem. 1955 Jan;212(1):165–177. [PubMed] [Google Scholar]
  7. GERGELY J. Muscle proteins and energy utilization. Ann N Y Acad Sci. 1959 Feb 6;72(12):538–554. doi: 10.1111/j.1749-6632.1959.tb44181.x. [DOI] [PubMed] [Google Scholar]
  8. GREY T. C., PERRY S. V. A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphatase. Biochem J. 1956 Sep;64(1):184–192. doi: 10.1042/bj0640184. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MUELLER H., PERRY S. V. The chromatography of the meromyosins on diethylaminoethylcellulose. Biochem J. 1961 Jul;80:217–223. doi: 10.1042/bj0800217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. PERRY S. V. The chromatography of L-myosin on diethylaminoethylcellulose. Biochem J. 1960 Jan;74:94–101. doi: 10.1042/bj0740094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. WEBER A. The ultracentrifugal separation of L-myosin and actin in an actomyosin sol under the influence of ATP. Biochim Biophys Acta. 1956 Feb;19(2):345–351. doi: 10.1016/0006-3002(56)90439-5. [DOI] [PubMed] [Google Scholar]

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

RESOURCES