Peiser L, Balinsky J B
J Exp Zool. 1982 Aug 10;222(2):107-12. doi: 10.1002/jez.1402220202.
Arginase from the liver of Xenopus laevis has been purified to homogeneity by heat treatment, acetone fractionation, and isoelectric focussing. The main component had an isoelectric point (I.E.P.) of 7.3; there is a minor component of I.E.P. 7.8. The molecular weight of the enzyme, as determined by gel filtration on Sephadex G200, is 76,000 daltons, substantially less than that of rat liver arginase studied concurrently. The molecular weight of the subunits, as determined by electrophoresis in sodium dodecyl sulfate, is 18,000 daltons, again less than that of rat liver arginase. The data indicate that Xenopus liver arginase, like rat liver arginase, is a tetramer. The molecular weight of arginase from adult Xenopus laevis corresponds to that from larval Rana esculenta.
通过热处理、丙酮分级分离和等电聚焦，从非洲爪蟾肝脏中纯化出了精氨酸酶，使其达到了均一性。主要成分的等电点（I.E.P.）为7.3；还有一个次要成分，其等电点为7.8。通过在Sephadex G200上进行凝胶过滤测定，该酶的分子量为76,000道尔顿，明显低于同时研究的大鼠肝脏精氨酸酶的分子量。通过在十二烷基硫酸钠中进行电泳测定，亚基的分子量为18,000道尔顿，同样低于大鼠肝脏精氨酸酶的分子量。数据表明，非洲爪蟾肝脏精氨酸酶与大鼠肝脏精氨酸酶一样，是一种四聚体。成年非洲爪蟾精氨酸酶的分子量与欧洲林蛙幼体精氨酸酶的分子量相当。
