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. 1990 Jul;93(3):1230–1234. doi: 10.1104/pp.93.3.1230

Purification and Properties of Arginase from Soybean, Glycine max, Axes

Jung Hoon Kang 1, Young Dong Cho 1
PMCID: PMC1062656  PMID: 16667583

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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