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

Abstract

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.

References

Jan 1, 1991·The International Journal of Biochemistry·J P Raffin, M Thebault
Jan 1, 1982·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·A Stankiewicz, W Makarewicz
Jan 1, 1983·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J SpychalaW Makarewicz
Apr 23, 2015·Biophysical Chemistry·Nicor Lengert, Barbara Drossel

Citations

Jul 1, 1975·Biochemical Medicine·A Stankiewicz, W Makarewicz
Jun 1, 1974·Biochemical Medicine·W Makarewicz, A Stankiewicz
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
Mar 21, 1974·Biochimica Et Biophysica Acta·C Y Lian, D R Harkness
Nov 4, 1969·Biochimica Et Biophysica Acta·L D Smith, D E Kizer
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
Potassium
Phosphate Measurement
Cations
AMP Deaminase
Nucleotide Deaminases
Enzymes for Treatment of Wounds and Ulcers
Deaminase
Potassium Ion
Muscle

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