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. 1987 Aug 14;146(3):945-52.
doi: 10.1016/0006-291x(87)90738-8.

Purification and characterization of a novel human angiogenic factor (h-AF)

Purification and characterization of a novel human angiogenic factor (h-AF)

K Schulze Osthoff et al. Biochem Biophys Res Commun. .

Abstract

Serum-free supernatants of the human melanoma cell line A-375/2 contain an angiogenic activity as detected by the chorioallantois membrane assay which does not induce proliferation of cultured endothelial cells. This human angiogenic factor (h-AF) was purified by immunoaffinity chromatography as well as by conventional chromatographic procedures. A monoclonal antibody designated 5F4 was raised against h-AF, which binds but does not neutralize angiogenic activity. h-AF consists of a protein at MW 67 kD which focuses at pH 5.0. By biological and biochemical criteria it is shown that h-AF differs from other known growth factors.

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