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Article

Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF.

The Journal of biological chemistry - 5 Jun 1992

Andersson M, Ostman A, Bäckström G, Hellman U, George-Nascimento C, Westermark B, Heldin C H

Abstract excerpt

Platelet-derived growth factor (PDGF) is a dimeric factor stabilized by disulfide bonds. Using an approach involving partial reduction of PDGF, we have identified the 2nd and 4th cysteine residues in the PDGF chains as the cysteine residues forming interchain disulfide bonds. Analysis of PDGF mutants in which the 2nd and 4th cysteine residues were mutated to serine residues revealed that the disulfide bonds are...

Topics

Amino Acid Sequence
Chromatography, High Pressure Liquid
DNA
Disulfides
Hydrolysis
Molecular Sequence Data
Mutation
Phosphorylation
Platelet-Derived Growth Factor
Precipitin Tests

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Cell Surface

Receptors, Platelet-Derived Growth Factor

Recombinant Proteins

Source

Identifiers

PMID: 1317862

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1317862-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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