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Comparative studies on muscle AMP-deaminase--II. Regulation by monovalent cations, ATP and orthophosphate of the enzyme from hen, frog and pikeperch muscle.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1979
Type
Research Support, Non-U.S. Gov't
Journal Article
Comparative Study
Volume
1979 / 62 : 371-4
Author
Stankiewicz A 1, Spychala J
Affiliation

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Doi
PMIDMESH
AMP Deaminase
Adenosine Triphosphate
Animals
Cations, Monovalent
Chickens
Enzyme Activation
Female
Fishes
Hydrogen-Ion Concentration
Kinetics
Muscles
Nucleotide Deaminases
Phosphates
Potassium
Rana esculenta
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.
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Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
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