Comparative studies on muscle AMP-deaminase--II. Regulation by monovalent cations, ATP and orthophosphate of the enzyme from hen, frog and pikeperch muscle.
作者信息
Stankiewicz A, Spychala J
机构信息
Department of Biochemistry, Medical School, Gdańsk, Poland.
出版信息
Comp Biochem Physiol B. 1979;62(4):371-4. doi: 10.1016/0305-0491(79)90105-6.
PMID:45554
Abstract
- Michaelis constants, maximum velocity and pH-dependence of the reaction catalysed by homogeneous AMP-deaminase preparations from hen, frog and pikeperch skeletal muscle were compared, as well as the influence of monovalent cations, ATP and inorganic phosphate. 2. ATP was found to activate the enzymes in the absence of K+ and at optimum (150 mM) KCl concentration. 3. Absolute dependence on potassium ions and considerable dependence of Km and Vmax on the kind of monovalent cation present in the medium were found for pikeperch enzyme.
摘要
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