EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A 41 KDA INSULIN-RECEPTOR TYROSINE KINASE DOMAIN

被引：9

作者：

KALLEN, RG ^{[1
]}

SMITH, JE ^{[1
]}

SHENG, ZF ^{[1
]}

TUNG, L ^{[1
]}

机构：

[1] UNIV PENN,SCH MED,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 168卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92365-7

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：

An active 41 kDa cytoplasmic domain of the insulin receptor tyrosine kinase(CIRK-41) encompassing amino acid residues 946 and 1303 of the native protein with an additional three amino acids(HAI) at the N-terminus has been overexpressed using the baculovirus pAC 373 expression system. The recombinant protein termed CIRK-41 has been purified to homogeneity. CIRK-41 was capable of autophosphorylation and up to 1.9 moles of phosphate were incorporated per mole of enzyme when it was incubated in the presence of 10 mM manganese chloride and 0.5 mM ATP. Autophosphorylation resulted in stimulation of CIRK-41 activity towards its exogenous substrate, indicating that CIRK-41 may be used as a model molecule to study the role of phosphorylation and dephosphorylation in the control of the insulin receptor tyrosine kinase activity. © 1990.

引用

页码：616 / 624

页数：9

共 30 条

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