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Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides.

Abstract：

:Synthetic peptides derived from the sequence surrounding tyrosine-857 in the human platelet-derived growth factor (PDGF) beta-receptor were used to elucidate the requirement for length and presence of negative and positively charged amino acids in substrates of the PDGF beta-receptor protein tyrosine kinase. The measured Km for the different peptides were all in the range 1-10 mM. A peptide of only five amino acids, lacking acidic amino acid residues, were found to be substrates for the receptor kinase. Ligand binding was found to stimulate the phosphorylation of peptides mainly by lowering the Km both for peptide and for ATP. Only minor changes in the Vmax occurred upon stimulation with PDGF. The reaction mechanism was found to be sequential, i.e. both the peptide and ATP have to bind to the enzyme before any product is released.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Rönnstrand L,Sorokin A,Engström U,Heldin CH

doi

10.1016/0006-291x(90)90669-e

subject

Has Abstract

pub_date

1990-03-30 00:00:00

pages

1333-40

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)90669-E

journal_volume

167

pub_type

杂志文章

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