Bergamini C M, Signorini M, Ferrari C, Poltronieri L, Rippa M
Biochem Int. 1983 Sep;7(3):353-60.
Incubation of skeletal muscle glycogen phosphorylase with sodium periodate's results into irreversible loss of enzyme activity. The rate of inactivation is influenced by the ionic strength of the medium and by the presence of caffeine, but not by nucleotides. During the reaction, cysteine residues slowly reactive towards DTNB are modified and the coenzyme is released. These results suggest the presence of cysteine residues at the protein site involved in the binding of the phosphate group of pyridoxal phosphate.
骨骼肌糖原磷酸化酶与高碘酸钠一起温育会导致酶活性不可逆丧失。失活速率受介质离子强度和咖啡因的存在影响，但不受核苷酸影响。在反应过程中，对半胱氨酸残基有缓慢反应活性的二硫代硝基苯甲酸（DTNB）被修饰，辅酶被释放。这些结果表明在参与磷酸吡哆醛磷酸基团结合的蛋白质位点存在半胱氨酸残基。
