Purification and Properties of Arginase from Soybean, Glycine max, Axes
Open Access
- 1 July 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 93 (3) , 1230-1234
- https://doi.org/10.1104/pp.93.3.1230
Abstract
Arginase (EC 3.5.3.1) was purified to homogeneity from cytosol of soybean, Glycine max, axes by chromatographic separations on Sephadex G-200, DEAE-sephacel, hydroxyapatite, and arginine-affinity columns. The molecular weight of the enzyme estimated by pore gradient gel electrophoresis was 240,000, while sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a single band at the molecular weight of 60,000. The optimal pH for activity was 9.5 and the Km value was 83 millimolar. The enzyme was stimulated by polyamines such as putrescine.This publication has 24 references indexed in Scilit:
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