Polishchuk S V, Brandt N R, Meyer H E, Varsányi M, Heilmeyer L M
Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Germany.
FEBS Lett. 1995 Apr 10;362(3):271-5. doi: 10.1016/0014-5793(95)00260-g.
Immunoblotting as well as enzyme assays demonstrate the presence of the self-glucosylating protein, glycogenin, in the protein-glycogen complex, in the sarcoplasmic reticulum and in phosphorylase kinase. In all three compartments glycogenin occurs in different, albeit, defined glucosylated forms, which upon deglucosylation are converted into a 42 kDa form. We suggest that phosphorylase kinase might have a dual function in glycogen biogenesis: firstly, control of glycogen degradation in the protein-glycogen complex via phosphorylation of glycogen phosphorylase b; secondly, regulation of glycogen biosynthesis on the sarcoplasmic reticular membranes via phosphorylation and thereby inhibition of glycogen synthase.
免疫印迹以及酶分析表明，在蛋白质 - 糖原复合物、肌浆网和磷酸化酶激酶中存在自糖基化蛋白糖原素。在所有这三个区室中，糖原素以不同但确定的糖基化形式存在，去糖基化后会转化为42 kDa的形式。我们认为磷酸化酶激酶在糖原生物合成中可能具有双重功能：首先，通过糖原磷酸化酶b的磷酸化控制蛋白质 - 糖原复合物中的糖原降解；其次，通过磷酸化从而抑制糖原合酶来调节肌浆网膜上的糖原生物合成。
