Plant Physiology 1990-Jul
Purification and Properties of Arginase from Soybean, Glycine max, Axes.
Kun registrerede brugere kan oversætte artikler
Log ind / Tilmeld
Linket gemmes på udklipsholderen
Nøgleord
Abstrakt
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 K(m) value was 83 millimolar. The enzyme was stimulated by polyamines such as putrescine.