Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1980 Aug 1;189(2):367–368. doi: 10.1042/bj1890367

Effects of storage on activity and subunit structure of rabbit skeletal-muscle AMP deaminase.

M Ranieri-Raggi, A Raggi
PMCID: PMC1162007  PMID: 7458918

Abstract

On storage, AMP deaminase is converted into a form exhibiting hyperbolic kinetics even at low KCl concentration. This effect results from cleavage of the enzyme subunit (mol.wt. 79 000) to a product of similar size to the component of approx. mol.wt. 70 000 present in trace amounts in AMP deaminase just prepared from fresh muscle.

Full text

PDF
367

Selected References

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

  1. Ashman L. K., Atwell J. L. AMP deaminase from rabbit skeletal muscle: the effect of monovalent cations on catalytic activity and molecular weight. Biochim Biophys Acta. 1972 Feb 28;258(2):618–625. doi: 10.1016/0005-2744(72)90253-7. [DOI] [PubMed] [Google Scholar]
  2. BENDALL J. R., DAVEY C. L. Ammonia liberation during rigor mortis and its relation to changes in the adenine and inosine nucleotides of rabbit muscle. Biochim Biophys Acta. 1957 Oct;26(1):93–103. doi: 10.1016/0006-3002(57)90059-8. [DOI] [PubMed] [Google Scholar]
  3. Boosman A., Sammons D., Chilson O. An investigation of the subunit structure and AMP-deaminases from rabbit and chicken muscle. Biochem Biophys Res Commun. 1971 Nov;45(4):1025–1032. doi: 10.1016/0006-291x(71)90440-2. [DOI] [PubMed] [Google Scholar]
  4. Coffee C. J., Kofke W. A. Rat muscle 5'-adenylic acid aminohydrolase. I. Purification and subunit structure. J Biol Chem. 1975 Sep 10;250(17):6653–6658. [PubMed] [Google Scholar]
  5. Ogasawara N., Goto H., Yamada Y., Yoshino M. Subunit structures of AMP deaminase isozymes in rat. Biochem Biophys Res Commun. 1977 Dec 7;79(3):671–676. doi: 10.1016/0006-291x(77)91164-0. [DOI] [PubMed] [Google Scholar]
  6. Rahim Z. H., Lutaya G., Griffiths J. R. Activation of AMP aminohydrolase during skeletal-muscle contraction. Biochem J. 1979 Oct 15;184(1):173–176. doi: 10.1042/bj1840173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ranieri-Raggi M., Raggi A. Regulation of skeletal muscle AMP deaminase: effects of limited proteolysis on the activity of the rabbit enzyme. FEBS Lett. 1979 Jun 1;102(1):59–63. doi: 10.1016/0014-5793(79)80928-x. [DOI] [PubMed] [Google Scholar]
  8. Ronca G., Raggi A., Ronca-Testoni S. Muscle AMP aminohydrolase. I. Some regulatory properties of rat skeletal muscle enzyme. Biochim Biophys Acta. 1968 Nov 19;167(3):626–629. doi: 10.1016/0005-2744(68)90058-2. [DOI] [PubMed] [Google Scholar]
  9. Scopes R. K., Penny I. F. Subunit sizes of muscle proteins, as determined by sodium dodecyl sulphate gel electrophoresis. Biochim Biophys Acta. 1971 May 25;236(2):409–415. doi: 10.1016/0005-2795(71)90221-2. [DOI] [PubMed] [Google Scholar]
  10. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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

RESOURCES