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聚焦层析分离人肝精氨酸酶同工酶组分
引用本文:汪迺经,吴厚生,沈荷芬,范行义.聚焦层析分离人肝精氨酸酶同工酶组分[J].复旦学报(医学版),1987(5).
作者姓名:汪迺经  吴厚生  沈荷芬  范行义
作者单位:上海医科大学基础医学部化学教研室 (汪迺经,沈荷芬),上海医科大学基础医学部病理生理学教研室 (吴厚生),上海医科大学基础医学部病理生理学教研室(范行义)
摘    要: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。

关 键 词:人肝  精氨酸酶类  同工酶  聚焦层析  聚丙烯酰胺凝胶电泳

ISOLATION OF HUMAN LIVER ARGINASE ISOENZYME FRACTIONS BY CHROMATOFOCUSING
Wang Naijing,Wu Honsheng,Snen Hefen,Fan Xingyi.ISOLATION OF HUMAN LIVER ARGINASE ISOENZYME FRACTIONS BY CHROMATOFOCUSING[J].Fudan University Journal of Medical Sciences,1987(5).
Authors:Wang Naijing  Wu Honsheng  Snen Hefen  Fan Xingyi
Abstract:Different arginase isoenzyme fractions from human liver extract were Isolated and purified by using DEAE Sephadex A-50 chromatography combined with chro-matofocusing. Two arginase isoenzyme fractions were obtained after ehromatofocu-sing, each of these fractions showed high arginase activity and appears to be homogeneous as examined by polyaerylamide gel electrophoresis. These arginase isoenzymes migrated to the cathode and the electrophoretic mobility patterns corresponded to those eluted from chromatofocusing. The molecular weights of the two subunits of A isoenzyme was determined by SDS-PAGE to be 3420dt and 22 400dt respectively. That for B isoenzyme were 34000dt and 22000dt respectively.
Keywords:liver of human  arginase  isoenzyme  chromatofocusing  electropho- resis  gel polyacrylamide
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