Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1960 Nov;77(2):262–271. doi: 10.1042/bj0770262

The inhibitory action of relaxing-factor preparations on the myofibrillar adenosine triphosphatase

G D Baird 1,2, S V Perry 1,2
PMCID: PMC1204981  PMID: 13686009

Full text

PDF
264

Selected References

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

  1. 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]
  2. BENDALL J. R. Muscle-relaxing factors. Nature. 1958 Apr 26;181(4617):1188–1190. doi: 10.1038/1811188a0. [DOI] [PubMed] [Google Scholar]
  3. BENDALL J. R. The relaxing effect of myokinase on muscle fibres; its identity with the Marsh factor. Proc R Soc Lond B Biol Sci. 1954 May 27;142(908):409–426. doi: 10.1098/rspb.1954.0033. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. BOZLER E., PRINCE J. T. The control of energy release in extracted muscle fibers. J Gen Physiol. 1953 Sep;37(1):53–61. doi: 10.1085/jgp.37.1.53. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. BRIGGS F. N., KALDOR G., GERGELY J. Participation of a dialyzable cofactor in the relaxing factor system of muscle. I. Studies with single glycerinated fibres. Biochim Biophys Acta. 1959 Jul;34:211–218. doi: 10.1016/0006-3002(59)90249-5. [DOI] [PubMed] [Google Scholar]
  7. CHAPPELL J. B., PERRY S. V. Biochemical and osmotic properties of skeletal muscle mitochondria. Nature. 1954 Jun 5;173(4414):1094–1095. doi: 10.1038/1731094a0. [DOI] [PubMed] [Google Scholar]
  8. GOODALL M. C., SZENT-GYORGYI A. G. Relaxing factors in muscle. Nature. 1953 Jul 11;172(4367):84–85. doi: 10.1038/172084a0. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. HASSELBACH W. Die Wechselwirkung verschiedener Nukleosidtriphosphate mit Aktomyosin in Gelzustand. Biochim Biophys Acta. 1956 May;20(2):355–368. doi: 10.1016/0006-3002(56)90297-9. [DOI] [PubMed] [Google Scholar]
  11. HASSELBACH W., WEBER H. H. Der Einfluss des MB-Faktors auf die Kontraktion des Fasermodells. Biochim Biophys Acta. 1953 May;11(1):160–161. doi: 10.1016/0006-3002(53)90021-3. [DOI] [PubMed] [Google Scholar]
  12. LORAND L. Adenosine triphosphate-creatine transphosphorylase as relaxing factor of muscle. Nature. 1953 Dec 26;172(4391):1181–1183. doi: 10.1038/1721181a0. [DOI] [PubMed] [Google Scholar]
  13. MARSH B. B. The effects of adenosine triphosphate on the fibre volume of a muscle homogenate. Biochim Biophys Acta. 1952 Sep;9(3):247–260. doi: 10.1016/0006-3002(52)90159-5. [DOI] [PubMed] [Google Scholar]
  14. MOLNAR J., LORAND L. Transphosphorylating enzymes and muscle relaxation. Nature. 1959 Apr 11;183(4667):1032–1034. doi: 10.1038/1831032a0. [DOI] [PubMed] [Google Scholar]
  15. PERRY S. V., CORSI A. Extraction of proteins other than myosin from the isolated rabbit myofibril. Biochem J. 1958 Jan;68(1):5–12. doi: 10.1042/bj0680005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. PERRY S. V. Relation between chemical and contractile function and structure of the skeletal muscle cell. Physiol Rev. 1956 Jan;36(1):1–76. doi: 10.1152/physrev.1956.36.1.1. [DOI] [PubMed] [Google Scholar]
  17. PERRY S. V. The protein components of the isolated myofibril. Biochem J. 1953 Aug;55(1):114–122. doi: 10.1042/bj0550114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PERRY S. V., ZYDOWO M. A ribonucleoprotein of skeletal muscle and its relation to the myofibril. Biochem J. 1959 Aug;72:682–690. doi: 10.1042/bj0720682. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. PORTER K. R., PALADE G. E. Studies on the endoplasmic reticulum. III. Its form and distribution in striated muscle cells. J Biophys Biochem Cytol. 1957 Mar 25;3(2):269–300. doi: 10.1083/jcb.3.2.269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. PORTZEHL H. Bewirkt das System Phosphokreatin-Phosphokinase die Erschlaffung des lebenden Muskels? Biochim Biophys Acta. 1957 Jun;24(3):474–482. doi: 10.1016/0006-3002(57)90235-4. [DOI] [PubMed] [Google Scholar]
  21. PORTZEHL H. Die Bindung des Erschlaffungsfaktors von Marsh an die Muskelgrana. Biochim Biophys Acta. 1957 Nov;26(2):373–377. doi: 10.1016/0006-3002(57)90019-7. [DOI] [PubMed] [Google Scholar]
  22. SLATER E. C., CLELAND K. W. The effect of calcium on the respiratory and phosphorylative activities of heart-muscle sarcosomes. Biochem J. 1953 Nov;55(4):566–590. doi: 10.1042/bj0550566. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Slater E. C. A comparative study of the succinic dehydrogenase-cytochrome system in heart muscle and in kidney. Biochem J. 1949;45(1):1–8. doi: 10.1042/bj0450001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. WEBER A. On the role of calcium in the activity of adenosine 5'-triphosphate hydrolysis by actomyosin. J Biol Chem. 1959 Oct;234:2764–2769. [PubMed] [Google Scholar]

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

RESOURCES