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• W1543880555 abstract "Abstract Rabbit liver arginase has been purified about 1,000-fold. The enzyme migrates as a single broad band during electrophoresis in disc gel, and gives a single precipitation line with specific antiserum when assayed by the immunodiffusion technique. However, chromatography of the purified enzyme on DEAE-cellulose columns reveals multiple active forms of identical molecular weight, which are eluted within a narrow range of molarity. The molecular weight determination by gel filtration yields a value of 110,000. The sedimentation coefficient is 5.9 S, as determined by sucrose gradient centrifugation. The rabbit arginase is almost completely inactivated after a long incubation in the presence of EDTA, without altering its immunoprecipitation pattern. It regains its initial activity when assayed in the presence of Mn++. Treatment of the rabbit liver arginase with 0.25% sodium dodecyl sulfate at pH 10, or incubation of the enzyme at pH 2, result in its rapid inactivation, when assayed in the absence of Mn++. However, when the inactivated enzyme is assayed in the presence of Mn++, a residual activity is observed, which corresponds to one component of 2.8 or 2.4 S after treatment with sodium dodecyl sulfate or at pH 2, respectively. The sodium dodecyl sulfate-dissociated enzyme has a molecular weight of 36,500, thus providing evidence for an oligomeric native structure, probably tetrameric, as previously reported for the rat liver arginase (Hirsch-Kolb, H., and Greenberg, D. M., J. Biol. Chem., 243, 6123 (1968)). The pH 2-dissociated enzyme migrates as two components of very close mobilities in 8 m urea gel electrophoresis, suggesting the occurrence of two kinds of subunits with similar molecular weight. This may account for the different chromatographic forms of the oligomeric native enzyme. The pH 2-dissociated enzyme regains at least 75% of its initial activity, when incubated at pH 8 in the presence of Mn++ and further assayed in the presence of Mn++. The reactivated enzyme appears to recover its native oligomeric structure, as suggested by its sedimentation coefficient (5.6 S), immunological properties, and electrophoretic mobility. If the pH 2-dissociated enzyme is incubated at pH 8 in the presence of EDTA, prior to assay, about 25% of the initial activity is observed, when assayed in the presence of Mn++. Under these conditions, the enzyme has a low sedimentation coefficient (2.7 S), like the dissociated enzyme, and gives rise to two bands migrating faster than the native enzyme in disc gel electrophoresis. Thus, the formation of the oligomeric structure seems to require manganous ions. Furthermore, the subunits are most probably active in the presence of Mn++, as suggested by the characteristics of the assay of dissociated enzymes and of enzyme reactivated at pH 8 in the presence of EDTA (high dilution, absence of lag period)." @default.
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• W1543880555 date "1972-02-01" @default.
• W1543880555 modified "2023-10-12" @default.
• W1543880555 title "Rabbit Liver l-Arginase" @default.
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• W1543880555 doi "https://doi.org/10.1016/s0021-9258(19)45638-x" @default.
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