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

Citation
M. Bobko et al., 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, Bioorganic & medicinal chemistry letters, 5(4), 1995, pp. 353-356
Citations number
9
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
ISSN journal
0960894X
Volume
5
Issue
4
Year of publication
1995
Pages
353 - 356
Database
ISI
SICI code
0960-894X(1995)5:4<353:CP-DOM>2.0.ZU;2-K
Abstract
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 requi red for efficient substrate turnover.