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用聚焦层析结合DEAE-Sephadex A-50离子交换层析,从正常人肝浸液中分离得两个精氨酸酶同工酶组分.经聚丙烯酰胺凝胶电泳(PAGE)鉴定从聚焦层析得到的第一峰同工酶组分为一条蛋白带,第二峰具有精氨酸酶活性的蛋白组分的主要蛋白带也极明显。各蛋白质成分向阴极电泳的前后顺序与从聚焦层析洗脱的先后次序一致。两型同工酶的比活力分别约为2050U/mg及790U/mg。用SDS-PAGE检测两型同工酶均由两种亚基组成,且分子量近似。
Two arginase isoenzyme fractions were isolated from normal human liver extracts by focused chromatography combined with DEAE-Sephadex A-50 ion exchange chromatography and identified by polyacrylamide gel electrophoresis (PAGE) The first peak isozyme component obtained by chromatography is one protein band, and the major protein band of the protein component having the arginase activity of the second peak is also conspicuous. The order of electrophoresis of each protein component to the cathode is in accordance with the order of elution from the focused chromatography. The specific activities of the two isozymes were about 2050 U / mg and 790 U / mg, respectively. Both isozymes were detected by SDS-PAGE and consisted of two subunits with similar molecular weights.