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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Published in | Biochemical and biophysical research communications Vol. 82; no. 2; pp. 492 - 497 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
1978
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Online Access | Get full text |
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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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(78)90901-4 |