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Properties of arginase immobilized in a fibrin clot
Author(s) -
Diez A.,
Campo ML,
Soler G.
Publication year - 1990
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1990.tb00095.x
Subject(s) - arginase , chemistry , fibrin , denaturation (fissile materials) , substrate (aquarium) , enzyme , covalent bond , biochemistry , immobilized enzyme , catalysis , chromatography , amino acid , arginine , organic chemistry , biology , nuclear chemistry , immunology , ecology
Rat liver arginase was covalently trapped in a fibrin clot. Among the physicochemical properties of the enzyme studied were Mn2+ requirement, pH behavior, temperature and time stability, effect of denaturing agents, and kinetic properties. The immobilized arginase showed the same substrate affinity as soluble arginase, but had higher stability at room temperature, was more resistant to denaturation, and had a higher catalytic activity at physiological pH. The properties so far examined may enhance the use of immobilized arginase in cancer therapy.