Abstract

Endothelial cell growth factor (ECGF), an anionic polypeptide mitogen, binds to immobilized heparin. The interaction between the acidic polypeptide and the anionic carbohydrate suggests a mechanism that is independent of ion exchange. Monoclonal antibodies to purified bovine ECGF inhibited the biological activity of ECGF in crude preparations of bovine brain. These data indicate that ECGF is the principal mitogen for endothelial cells from bovine brain, that heparin affinity chromatography may be used to purify and concentrate ECGF, and that the affinity of ECGF for heparin may have structural and perhaps biological significance.

Keywords

HeparinAffinity chromatographyEndothelial stem cellBiochemistryMonoclonal antibodyCellBiological activityGrowth factorChemistryAntibodyBiologyCell biologyEnzymeImmunologyReceptorIn vitro

MeSH Terms

AnimalsAntibodiesMonoclonalBrain ChemistryCattleCell DivisionChromatographyAffinityEndothelial Growth FactorsEndotheliumGrowth SubstancesHeparinIon Exchange

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Publication Info

Year
1984
Type
article
Volume
225
Issue
4665
Pages
932-935
Citations
387
Access
Closed

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Citation Metrics

387
OpenAlex
3
Influential
264
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Cite This

Thomas Maciag, Tevie Mehlman, Robert Friesel et al. (1984). Heparin Binds Endothelial Cell Growth Factor, the Principal Endothelial Cell Mitogen in Bovine Brain. Science , 225 (4665) , 932-935. https://doi.org/10.1126/science.6382607

Identifiers

DOI
10.1126/science.6382607
PMID
6382607

Data Quality

Data completeness: 81%