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PubMed · 1008818

Arginase from human full-term placenta.

R Porta·C Esposito·A Martin·G D Pietra
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Abstract

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.

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ArginaseChromatography, GelEnzyme ActivationHumansManganeseMolecular WeightPlacentaJournal Article

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R Porta, C Esposito, A Martin, G D Pietra. 1976-12-01. Arginase from human full-term placenta.. https://doi.org/10.1042/bj1590579

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