Binding Properties of Horse Colostral Immunoglobulins to Protein A-Sepharose CL-4B

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  • SHIMAZAKI Kei-ichi
    Laboratory of Dairy Chemistry, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine
  • NAKAJIMA Hideki
    Laboratory of Dairy Chemistry, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine

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Other Title
  • ウマ初乳免疫グロブリンのプロテインA一セファローズへの結合性
  • ウマ ショニュウ メンエキ グロブリン ノ プロティン A セファローズ ヘ

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Description

Although horse immunoglobulins from serum have been utilized for medical use such as anti-toxin preparations, their physiological and biological properties, apart from the antigen-antibody reaction, are little known. One of the biological properties possessed by immunoglobulin molecules is their specific affinity to Staphylococcal Protein A. In the cases of immunoglobulins of other animals such as human, rat, mouse, rabbit etc., preparation and quantitative assay of immunoglobulins in serum, milk and other secretions have been carried out based on their specific interactions with immobilized Protein A. However, such techniques are rarely applied to horse immunoglobulins, due to the lack of basic information on the binding properties to Protein A. The purpose of this study is to investigate the binding properties of horse colostral immunoglobulin to Protein A.

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