INVITRO PHOSPHORYLATION OF MOUSE OSTEOPONTIN EXPRESSED IN ESCHERICHIA-COLI

被引：43

作者：

ASHKAR, S ^{[1
]}

TEPLOW, DB ^{[1
]}

GLIMCHER, MJ ^{[1
]}

SAAVEDRA, RA ^{[1
]}

机构：

[1] BRIGHAM & WOMENS HOSP,CTR NEUROL DIS,BOSTON,MA 02115

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 191卷 / 01期

关键词：

D O I：

10.1006/bbrc.1993.1193

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To understand the role of post-translational modifications on the structure and function of osteopontin, a secreted glycosylated phosphoprotein, we expressed mouse osteopontin in E. coli as a fusion protein with glutathione-S-transferase (GST). The purified fusion protein was cleaved by factor Xa generating GST (26 kDa) and recombinant osteopontin (60 kDa). The fusion protein was phosphorylated in vitro by cytosolic, microsomal, and casein kinase II fractions from mouse kidney homogenates. The fusion protein and recombinant osteopontin were also phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. The suitability of the fusion and recombinant proteins as model substrates for the study of the function(s) and post-translational modifications of osteopontin is discussed. © 1993 Academic Press, Inc.

引用

页码：126 / 133

页数：8

共 33 条

[1]

CASTAGNOLA P, 1991, J BIOL CHEM, V266, P9944

[2]

CRAIG AM, 1989, J BIOL CHEM, V264, P9682

[3] PHOSPHORYLATION OF BOVINE HORMONE-SENSITIVE LIPASE BY THE AMP-ACTIVATED PROTEIN-KINASE - A POSSIBLE ANTILIPOLYTIC MECHANISM [J].