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Isolation and partial characterization of a soluble oncofetal antigen from murine and human amniotic fluids

✍ Scribed by Adel L. Barsoum; Joseph H. Coggin Jr.

Publisher
John Wiley and Sons
Year
1991
Tongue
French
Weight
550 KB
Volume
48
Category
Article
ISSN
0020-7136

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✦ Synopsis

Abstract

A soluble (cell‐free) oncofetal antigen (OFA) was detected in murine and human amniotic fluids by immunostaining with the murine monoclonal antibody (MAb 115) produced by syngeneic immunization with mid‐gestational mouse fetal cells. OFA was purified from the amniotic fluids by ammonium sulfate precipitation at 30–70% saturation, followed by successive gel chromatography of the OFA‐containing fraction on Sephacryl‐S300 HR, Q‐and S‐Sepharoses and lentil lectin agarose. The fraction eluted from the lentil lectin column gave a single band on SDS‐PAGE of the same molecular weight as the membrane‐bound OFA found on both fetal and tumor tissues of humans and several rodents. Both soluble and membrane‐bound OFAs share several chemical characteristics, including binding to lentil lectin and wheat‐germ agglutlnin, molecular weight (44 kDa) and pI (6.8). Mild Periodate oxidation of OFA did not affect its binding to MAb 115 in an enzyme‐linked immunosorbent assay, indicating that the reactive epitope is a peptide.

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