Separation and characterization of two bovine alpha 1-fetoprotein molecular variants by concanavalin A-Sepharose chromatography

Two molecular variants of bovine alpha 1-fetoprotein were separated by affinity chromatography of fetal calf serum on a concanavalin A-Sepharose column. Radialimmunodiffusion assay of bovine alpha 1-fetoprotein revealed that 29% of the alpha 1-fetoprotein in fetal serum lacked concanavalin A-binding...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 82; no. 2; pp. 492 - 497
Main Authors Lai, P.C.W., Lorscheider, F.L.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 1978
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Summary:Two molecular variants of bovine alpha 1-fetoprotein were separated by affinity chromatography of fetal calf serum on a concanavalin A-Sepharose column. Radialimmunodiffusion assay of bovine alpha 1-fetoprotein revealed that 29% of the alpha 1-fetoprotein in fetal serum lacked concanavalin A-binding activity whilst 71% of the alpha 1-fetoprotein was capable of binding to the lectin. These two bovine alpha 1-fetoprotein variants show antigenic identity suggesting that the polypeptide chain rather than the carbohydrate moiety of the alpha 1-fetoprotein molecule is the antigenic determinant.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(78)90901-4