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Protein phosphorylation of lysosomal arylsulfatase B in normal and leukemic leukocytes
Author(s) -
Uehara Yoshio,
Gasa Shinsei,
Makita Akira,
Sakurada Keisuke,
Miyazaki Tamotsu
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81048-1
Subject(s) - phosphorylation , arylsulfatase a , serine , threonine , arylsulfatase , sulfatase , biochemistry , chemistry , chronic myelogenous leukemia , microbiology and biotechnology , leukemia , biology , enzyme , immunology
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 32 P 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.