
Properties of immobilized AMP-aminohydrolase from rabbit muscles are studied. The enzyme retains its activity for a year, is stable under manifold treatment with the substrate or under single treatment with 1 M NaCl which contains 50% ethylene glycol or 10% isopropanol and under treatment with 5 M K2 HPO4 (pH 8.5). The established pH-optimum (6.5-7.0) and the temperature optimum (30-40 degrees C) for immobilized AMP-aminohydrolase as well as inhibition of its activity by Co2+, Cd2+, Zn2+ and n-chloromercury benzoate indicate similarity of its properties with those of the purified enzyme.
Time Factors, Muscles, Hydrogen-Ion Concentration, In Vitro Techniques, Enzymes, Immobilized, AMP Deaminase, Substrate Specificity, Kinetics, Nucleotide Deaminases, Animals, Rabbits
Time Factors, Muscles, Hydrogen-Ion Concentration, In Vitro Techniques, Enzymes, Immobilized, AMP Deaminase, Substrate Specificity, Kinetics, Nucleotide Deaminases, Animals, Rabbits
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