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<p>Natural antibodies are antibodies present in the sera of all individuals in the absence of any immunization. Carbohydrate-binding antibodies are a very important part of such antibodies and are considered molecules for the recognition and&#xa0;removal of dysfunctional or malignant cells. In this regard, carbohydrate-specific antibodies in donor plasma can be considered a source for the preparation of such antibodies as potential&#xa0;therapeutic agents for the prevention of tumor and viral diseases. A new approach in affinity chromatography was used to purify carbohydrate-specific antibodies from the IgG fraction of human plasma. The affinity carrier was prepared by attaching milk glycoproteins to a P10 polyacrylamide matrix using glutaric dialdehyde. In contrast to methods using the direct binding of different sugars, this approach is simpler and does not lead to the disruption of antigenic determinants as a result of their covalent binding. Using this approach, 3–4&#xa0;mg of specific antibodies were obtained from 150&#xa0;mg of the IgG fraction.</p>

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Antibodies to Carbohydrates, Affinity Purification with Milk Glycoproteins

  • 期刊论文

  • 发表日期：

    2025年11月24日

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  • Varduhi A. Hovhannisyan,
  • Gayane G. Poghosyan,
  • Vardan K. Gasparyan

摘要

Natural antibodies are antibodies present in the sera of all individuals in the absence of any immunization. Carbohydrate-binding antibodies are a very important part of such antibodies and are considered molecules for the recognition and removal of dysfunctional or malignant cells. In this regard, carbohydrate-specific antibodies in donor plasma can be considered a source for the preparation of such antibodies as potential therapeutic agents for the prevention of tumor and viral diseases. A new approach in affinity chromatography was used to purify carbohydrate-specific antibodies from the IgG fraction of human plasma. The affinity carrier was prepared by attaching milk glycoproteins to a P10 polyacrylamide matrix using glutaric dialdehyde. In contrast to methods using the direct binding of different sugars, this approach is simpler and does not lead to the disruption of antigenic determinants as a result of their covalent binding. Using this approach, 3–4 mg of specific antibodies were obtained from 150 mg of the IgG fraction.