CD45 PROTEIN-TYROSINE-PHOSPHATASE - DETERMINATION OF MINIMAL PEPTIDE LENGTH FOR SUBSTRATE RECOGNITION AND SYNTHESIS OF SOME TYROSINE-BASED ELECTROPHILES AS POTENTIAL ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITORS

被引：9

作者：

BOBKO, M

WOLFE, HR

SAHA, A

DOLLE, RE

FISHER, DK

HIGGINS, TJ

机构：

[1] STERLING WINTHROP PHARMACEUT RES DIV, DEPT ANALYT SCI, COLLEGEVILLE, PA 19426 USA

[2] STERLING WINTHROP PHARMACEUT RES DIV, DEPT IMMUNOL, COLLEGEVILLE, PA 19426 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1995年 / 5卷 / 04期

关键词：

D O I：

10.1016/0960-894X(95)00034-Q

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Using fyn PTK as a template, a series of phosphopeptides 1-11 spanning in length from 1-14 amino acids was prepared. Kinetic evaluation of 1-11 suggest that CD45 does not have a strong preference for its N- or C-terminal amino acids and that extended phosphopeptides are not required for efficient substrate turnover.

引用

页码：353 / 356

页数：4

共 9 条

[1]

BOLEN JB, 1991, ADV CANCER RES, V57, P103

[2] CATALYTIC DOMAINS OF THE LAR AND CD45 PROTEIN TYROSINE PHOSPHATASES FROM ESCHERICHIA-COLI EXPRESSION SYSTEMS - PURIFICATION AND CHARACTERIZATION FOR SPECIFICITY AND MECHANISM [J].