PMID: 45554Jan 1, 1979

Comparative studies on muscle AMP-deaminase--II. Regulation by monovalent cations, ATP and orthophosphate of the enzyme from hen, frog and pikeperch muscle

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
A Stankiewicz, J Spychala


1. 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.


Jan 1, 1991·The International Journal of Biochemistry·J P Raffin, M Thebault
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Jul 1, 1975·Biochemical Medicine·A Stankiewicz, W Makarewicz
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Apr 14, 1971·Biochimica Et Biophysica Acta·K MurakamiK Tsushima
Oct 15, 1972·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M Zydowo, J Purzycka-Preis
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Mar 5, 1971·FEBS Letters·G Mor
Aug 1, 1962·Comparative Biochemistry and Physiology·W Makarewicz, M Zydowo
Mar 22, 1965·Biochimica Et Biophysica Acta·B CUNNINGHAM, J M LOWENSTEIN

Related Concepts

Enzymes, antithrombotic
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