[Physico-chemical properties of guinea pig liver arginase (author's transl)].
Arginase (E.C. 3.5.3.1) the enzyme which catalyses the hydrolysis of arginine to ornithine and urea has been investigated in guinea pig liver in relation to the kinetic constants of its substrate and inhibitors as well as to other physico-chemical properties. The results show that the enzyme has Km value of 19.6 mM for its substrate L-arginine and is competitively inhibited by one of its reaction products, the L-ornithine, and also by L-lysine and diaminopymelic acid. Optimal activity of the enzyme occurs at 10.5 pH and maximal stability in the range of 6.5 to 7.5 pH. The mentioned arginase exhibits temperature dependent activity and stability, being 64 degrees C (15 min and pH 7.5) the half-inactivation temperature. An increase in the activity and temperature stability of the enzyme, when previously activated by heating for 5 min at 45 degrees C in the presence of 10 mM MnCl2, has been achieved.
D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004789:Enzyme Activation; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008345:Manganese / Q000494:pharmacology; D013696:Temperature
D008345:Manganese; D001119:Arginase
Propiedades físico-químicas de la arginasa de hígado de cobaya.