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

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Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides. / Rönnstrand, Lars; Sorokin, Andrey; Engström, Ulla; Heldin, Carl-Henrik.

I: Biochemical and Biophysical Research Communications, Vol. 167, Nr. 3, 1990, s. 1333-1340.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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TY - JOUR

T1 - Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides

AU - Rönnstrand, Lars

AU - Sorokin, Andrey

AU - Engström, Ulla

AU - Heldin, Carl-Henrik

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

KW - Platelet-Derived Growth Factor Recombinant Proteins/metabolism Substrate Specificity

KW - Cell Surface/metabolism Receptors

KW - Amino Acid Sequence Humans Kinetics Molecular Sequence Data Oligopeptides/chemical synthesis/metabolism/pharmacology Phosphorylation Platelet-Derived Growth Factor/metabolism Protein Kinases/metabolism Receptors

M3 - Article

VL - 167

SP - 1333

EP - 1340

JO - Biochemical and Biophysical Research Communications

T2 - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 1090-2104

IS - 3

ER -