Studies on antigenicity of glycoprotein and protein fractions purified from erythrocyte membrane by phenol extraction method

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  • Arimori Shigeru
    Division of Immunology, Department of internal Medicine, Medical School, Okayama University
  • Shinozawa Shinya
    Deivision of Pharmacy, Okayama University Hospital

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Other Title
  • Phenol 抽出法で精製した赤血球膜糖蛋白と蛋白分画の抗膜抗体に対する抗原性の検討
  • Phenol抽出法で精製した赤血球膜糖蛋白と蛋白分画の抗膜抗体に対する抗原性の検討(速報)
  • Phenol チュウシュツホウ デ セイセイシタ セッケッキュウ マク トウ

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Abstract

The glycoproteins were purified using cold phenol method from erythrocyte membrane solubilized with lithium diiodosalicylate. Two bands, one was broad the other narrow, were stained on 1% SDS, 5% polyacrylamide gel with both Coomassie brilliant blue and periodic acid Schiff stainings, been calculated their molecular weights at 100000 and 55000 daltons, respectively. The protein fraction, which was obtained from residue of glycoprotein extraction, and the glycoproteins made a converging arc against the anti-membrane antibody in the micro-Ouchterlony agar. The glycoproteins only produced another fine precipitation simultaneously. All of these precipitations proved to contain the protein, glucose and lipid. Although further elucidation should be undertaken, these results suggested that antigens against the antimembrane antibody do exist in both glycoprotein and protein fractions of erythrocyte membrane.

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