Gold A H, Dickemper D, Haverstick D M
Mol Cell Biochem. 1979 May 6;25(1):47-59. doi: 10.1007/BF00211141.
Liver glycogen synthase b phosphatase, chromatographically separable from phosphorylase a phosphatase, is decreased in 48-hour alloxan diabetic rats. The phosphatase activities are measured in an in vitro system using exogenous isolated phospho-enzyme as substrates with added phosphatases. Synthase and phosphorylase phosphatases were shown to have differential catalytic properties by their reactivity in the presence of Pi, the heat-stable inhibitor of phosphorylase phosphatase and after incubation with added cAMP-dependent protein kinase.
肝糖原合酶b磷酸酶可通过色谱法与磷酸化酶a磷酸酶分离，在四氧嘧啶诱导糖尿病48小时的大鼠中含量降低。磷酸酶活性在体外系统中测定，该系统使用外源性分离的磷酸化酶作为底物，并添加磷酸酶。通过糖原合酶和磷酸化酶磷酸酶在无机磷酸盐（磷酸化酶磷酸酶的热稳定抑制剂）存在下的反应性，以及与添加的环磷酸腺苷依赖性蛋白激酶孵育后的反应性，显示它们具有不同的催化特性。
