Uehara Y, Gasa S, Makita A, Sakurada K, Miyazaki T
FEBS Lett. 1986 Nov 24;208(2):352-6. doi: 10.1016/0014-5793(86)81048-1.
An acidic variant form of arylsulfatase B from normal leukocytes and chronic myelogenous leukemia (CML) leukocytes was found to be phosphorylated at its serine and threonine residues through in vivo phosphorylation with 32Pi. However, the predominant phosphorylation site was serine in normal cells, in contrast to threonine in CML cells. A cyclic AMP-dependent protein kinase was responsible for phosphorylation of the sulfatase of CML cells.
通过用³²P₁进行体内磷酸化，发现来自正常白细胞和慢性粒细胞白血病（CML）白细胞的芳基硫酸酯酶B的一种酸性变体形式在其丝氨酸和苏氨酸残基处发生了磷酸化。然而，正常细胞中主要的磷酸化位点是丝氨酸，而CML细胞中则是苏氨酸。一种环磷酸腺苷依赖性蛋白激酶负责CML细胞硫酸酯酶的磷酸化。
