doi: 10.1016/0020-711x(78)90018-6.
Temperature- and pH-induced changes of the enzyme-substrate affinity and the reaction velocity catalysed by rabbit skeletal muscle AMP-Deaminase
- PMID: 25207
- DOI: 10.1016/0020-711x(78)90018-6
Item in Clipboard
Temperature- and pH-induced changes of the enzyme-substrate affinity and the reaction velocity catalysed by rabbit skeletal muscle AMP-Deaminase
Int J Biochem.
1978.
No abstract available
Similar articles
-
pH-dependent cold lability of rabbit skeletal muscle AMP deaminase.Biochim Biophys Acta. 1983 Feb 15;742(3):623-9. doi: 10.1016/0167-4838(83)90281-9. Biochim Biophys Acta. 1983. PMID: 6838893
-
Regulatory properties of AMP deaminase isoenzymes from rabbit red muscle.Biochem J. 1987 Mar 15;242(3):875-9. doi: 10.1042/bj2420875. Biochem J. 1987. PMID: 3593281 Free PMC article.
-
Adenylate metabolism in the heart. Regulatory properties of rabbit cardiac adenylate deaminase.Biochem J. 1979 Aug 15;182(2):361-6. doi: 10.1042/bj1820361. Biochem J. 1979. PMID: 41518 Free PMC article.
-
[AMP-aminohydrolase of the brain and other organs and the regulation of its activity].Vopr Biokhim Mozga. 1974;9:251-72. Vopr Biokhim Mozga. 1974. PMID: 4620815 Review. Russian.
-
[Effect of uni- and divalent cations on creatine kinase and AMP-deaminase activity].Nauchnye Doki Vyss Shkoly Biol Nauki. 1979;(10):5-15. Nauchnye Doki Vyss Shkoly Biol Nauki. 1979. PMID: 228776 Review. Russian. No abstract available.
Cited by
-
Evidence for sequential expression of multiple AMP deaminase isoforms during skeletal muscle development.Proc Natl Acad Sci U S A. 1987 Apr;84(8):2345-9. doi: 10.1073/pnas.84.8.2345. Proc Natl Acad Sci U S A. 1987. PMID: 3470799 Free PMC article.