Protein phosphorylation of lysosomal arylsulfatase B in normal and leukemic leukocytes

FEBS Letters

Sakurada, Keisuke²  Miyazaki, Tamotsu²  Gasa, Shinsei¹  Uehara, Yoshio²  Makita, Akira¹ 

[1] Biochemistry Laboratory, Cancer Institute, Hokkaido University School of Medicine, Sapporo 060, Japan;Third Department of Internal Medicine, Cancer Institute, Hokkaido University School of Medicine, Sapporo 060, Japan

关键词: Arylsulfatase B (Human leukocyte) Chronic myelogenous leukemia Phosphorylation cyclic AMP dependence Protein kinase Lysosome;   

DOI  :  10.1016/0014-5793(86)81048-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ³²P_i. 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.

【 授权许可】

Unknown