Removing of unnecessary antibodies by affinity chromatography on immobilized allo A lectin-binding glycoproteins.
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概要
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A method for removing of unnecessary antibodies was developed. Allo A lectin-Sepharose 4B and its binding serum glycoproteins were crosslinked by the dimethyl suberimidate. The antibodies on the market were purified by affinity chromatography on glycoproteins-allo A-Sepharose. By the method, anti-α1-antitrypsin, anti-hemopexin and anti-transferrin were obtained from the eluted fraction, and anti-retinol binding protein was obtained from the nonretarded fraction. On the other hand, anti-factor I and anti-Gc-globulin were obtained from both fractions. The method proved to be excellent for removing unnecessary antibodies from so called monospecific antibody on the market.
- 日本電気泳動学会の論文
日本電気泳動学会 | 論文
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