AUTOMATED NONISOTOPIC ASSAY FOR PROTEIN TYROSINE KINASE AND PROTEIN TYROSINE PHOSPHATASE-ACTIVITIES

被引：18

作者：

BABCOOK, J ^{[1
]}

WATTS, J ^{[1
]}

AEBERSOLD, R ^{[1
]}

ZILTENER, HJ ^{[1
]}

机构：

[1] UNIV BRITISH COLUMBIA,BIOMED RES CTR,2222 HLTH SCI MALL,VANCOUVER V6T 1Z3,BC,CANADA

来源：

ANALYTICAL BIOCHEMISTRY | 1991年 / 196卷 / 02期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0003-2697(91)90461-2

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A sensitive, automated, and nonisotopic assay for protein-tyrosine kinases and phosphatases has been developed. The assay uses commercially available antiphosphotyrosine monoclonal antibodies and the recently developed particle concentration immunofluorescence immunoassay technology. The assay is specific for phosphotyrosine residues, can be performed faster, and is at least 100-fold more sensitive than the current standard filter type radioassay. Myelin basic protein and a synthetic peptide corresponding to the autophosphorylation site of p56lck performed equally well in the detection of p56lck kinase activity. Myelin basic protein phosphorylated on tyrosine residues by p56lck was successfully used as substrate in the detection of phosphatase activity and vanadate or molybdate were shown to inhibit the phosphatase activity. The assay is particularly useful for the rapid detection of enzyme activities in column fractions from biochemical procedures steps and also for screening of large numbers of potential inhibitors or activators of protein-tyrosine kinases and phosphatases. © 1991.

引用

页码：245 / 251

页数：7

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