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Solubilized Glycoprotein from Human Erythrocyte Membranes Possessing Blood Group A, B and H Activity 1
Author(s) -
Whittemore N. B.,
Trabold N. C.,
Reed C. F.,
Weed R. I.
Publication year - 1969
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1969.tb00398.x
Subject(s) - lysis , glycoprotein , glycolipid , red blood cell , distilled water , membrane glycoproteins , fractionation , membrane , biochemistry , solubilization , erythrocyte membrane , chemistry , membrane protein , chromatography , biology
Summary. Human erythrocyte ghosts where prepared by osmotic lysis and washed thoroughly with deionized distilled water. The resultant stroma were extracted twice with n‐butanol producing 81.8 % ± 2.7 solubilization of the membrane protein. The initial extract contained 5 % of the lipid present in intact ghosts. The second extract contained no detectable lipids. The solubilized glycoprotein possessed A, B and H blood group activity comparable to that of the intact ghosts at the same protein concentration. Fractionation studies suggested that the maximum serological activity was associated with a high molecular weight structure. In contrast to most previous work demonstrating A, B and H blood group activities to be exhibited by erythrocyte glycolipids this study reports these blood group specificities to be present in human erythrocyte membrane glycoprotein.