Purification of porcine heart latent protein phosphatase Fc.M.

M D Schuchard, S D Killilea
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引用次数: 1

Abstract

Latent protein phosphatase, Fc.M, was purified from porcine heart extracts by a procedure involving precipitation at pH 5.0, DEAE-Sephacel chromatography, ammonium sulfate fractionation, chromatography on phenyl-Sepharose, Biogel-A 0.5m and poly-L-lysine-agarose. The purified enzyme had a specific activity of 12,200 nanomoles of phosphate released from phosphorylase a/mg protein when assayed following activation by pretreatment with Mn++ and trypsin in the presence of 0.2 M NaCl. The enzyme is a heterodimer of 66 kDa composed of a catalytic (37 kDa) and a modulator (31 kDa) subunit.

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猪心脏潜伏蛋白磷酸酶的纯化。
潜伏蛋白磷酸酶经pH 5.0沉淀、DEAE-Sephacel层析、硫酸铵分馏、苯基- sepharose层析、Biogel-A 0.5m层析和聚l-赖氨酸-琼脂糖层析,从猪心脏提取物中纯化出M。在0.2 M NaCl的作用下,用Mn++和胰蛋白酶预处理磷酸化酶a释放的磷酸比活性为12200纳米摩尔/mg蛋白。该酶是由催化亚基(37 kDa)和调节亚基(31 kDa)组成的异二聚体,分子量为66 kDa。
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