Hammar L
Agents Actions. 1983 Apr;13(2-3):246-9. doi: 10.1007/BF01967343.
Mouse mastocytoma histidine decarboxylase is decreased in activity when, in crude preparations, incubated with a cAMP-dependent protein kinase. This effect was not seen with purified preparations of the histidine decarboxylase (specific activity 7-13 mumol X mg-1 X h-1). Further, no incorporation of 32P from AT32P during incubation of this enzyme with the protein kinase could be demonstrated. Therefore, if protein phosphorylation operates in the regulation of the histidine decarboxylase, factors removed during the purification must be involved.
当粗制制剂中的小鼠肥大细胞瘤组氨酸脱羧酶与一种依赖环磷酸腺苷(cAMP)的蛋白激酶一起孵育时,其活性会降低。而对于纯化的组氨酸脱羧酶制剂(比活性为7 - 13 μmol·mg⁻¹·h⁻¹),则未观察到这种效应。此外,在该酶与蛋白激酶孵育期间,无法证明有来自ATP³²P的³²P掺入。因此,如果蛋白磷酸化在组氨酸脱羧酶的调节中起作用,那么在纯化过程中去除的因子必定参与其中。