Arginase from human full-term placenta
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Arginase was purified about 1800-fold from extracts of human full-term placenta; the enzyme appeared to be homogenous by disc electrophoresis and molecular-sieve chromatography. The mol. wt. determination by gel filtration and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis yielded a value of 70000 for the most pure and the partially purified enzyme. The human placenta arginase is a metalloenzyme with an optimum pH of 9.1. The Km for L-arginine is 27 mM. L-Ornithine and L-lysine show competitive inhibition with Ki values of 6.3 and 14 mM respectively.
1999 ◽
Vol 181
(1)
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pp. 91-99
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1984 ◽
Vol 62
(10)
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pp. 964-969
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1998 ◽
Vol 64
(2)
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pp. 789-792
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