Periodate inactivates muscle glycogen phosphorylase by modifying the enzyme active site.
Periodate inactivates muscle glycogen phosphorylase by modifying the enzyme active site.
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高碘酸盐通过修饰酶活性位点使肌糖原磷酸化酶失活。
DOI：
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发表时间：
1983
期刊：
影响因子：
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通讯作者：
M. Rippa
中科院分区：
文献类型：
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作者：
C. Bergamini;M. Signorini;C. Ferrari;L. Poltronieri;M. Rippa
骨骼肌糖原磷酸化酶与高碘酸钠一起孵育会导致酶活性不可逆转地丧失。失活速率受介质的离子强度和咖啡因的存在的影响，但不受核苷酸的影响。在反应过程中，对DTNB缓慢反应的半胱氨酸残基被修饰，辅酶被释放。这些结果表明，半胱氨酸残基的存在下，参与磷酸吡哆醛的磷酸基团的结合的蛋白质位点。
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.