USE OF HYDROPHILIC INTERACTION CHROMATOGRAPHY FOR THE STUDY OF TYROSINE PROTEIN-KINASE SPECIFICITY

被引：30

作者：

BOUTIN, JA ^{[1
]}

ERNOULD, AP ^{[1
]}

FERRY, G ^{[1
]}

GENTON, A ^{[1
]}

ALPERT, AJ ^{[1
]}

机构：

[1] POLYLC INC,COLUMBIA,MD 21045

来源：

JOURNAL OF CHROMATOGRAPHY-BIOMEDICAL APPLICATIONS | 1992年 / 583卷 / 02期

关键词：

D O I：

10.1016/0378-4347(92)80546-3

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

A new HPLC method has been developed to assay tyrosine protein kinase activity. Using hydrophilic interaction chromatography, it is possible to resolve the four components of the incubation medium: substrate peptide, [P-32]phosphorylated peptide, unreacted [gamma-P-32]ATP, and P-32-labelled inorganic phosphate. ATP interacts so strongly with the stationary phase material that it can be removed selectively from the incubation medium with solid-phase extraction cartridges packed with the same type of material. The three remaining components of interest can then be resolved by reversed-phase or hydrophilic interaction HPLC. This procedure permits the evaluation of almost every type of peptide as a substrate of tyrosine protein kinase.

引用

页码：137 / 143

页数：7

共 19 条

[1] SYNTHETIC PEPTIDES AS MODEL SUBSTRATES FOR THE STUDY OF THE SPECIFICITY OF THE POLYCATION-STIMULATED PROTEIN PHOSPHATASES [J].