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Isolation and partial characterization of a soluble oncofetal antigen from murine and human amniotic fluids
Author(s) -
Barsoum Adel L.,
Coggin Joseph H.
Publication year - 1991
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910480216
Subject(s) - oncofetal antigen , epitope , lectin , microbiology and biotechnology , monoclonal antibody , antigen , amniotic fluid , biology , concanavalin a , biochemistry , antibody , chemistry , fetus , in vitro , immunology , genetics , tumor associated antigen , pregnancy
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.