Anti-Rho(D) IgG binds to band 3 glycoprotein of the human erythrocyte membrane.
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چکیده
منابع مشابه
Anti-Rho(D) IgG binds to band 3 glycoprotein of the human erythrocyte membrane.
Alkali-extracted erythrocyte ghost membranes from Rho(D)-positive and Rho(D)-negative donors were incubated with human immune anti-Rho(D) IgG and nonimmune IgG. After sensitization with IgG, the integral membrane proteins were solubilized in Brij 36T nonionic detergent and chromatographed by gel filtration. There was a distinct resolution of IgG into free and membrane-complexed forms. The IgG-c...
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The phenomenon of molecular mimicry was found previously for Citrobacter braakii O37, which shared epitopes with human and horse erythrocytes. The aim of this study was to elucidate the basis of the serological cross-reactivity between anti-C. braakii O37 serum and human erythrocytes. The experiments involved analyzing the epitope on the human erythrocyte membrane, that could be recognized by a...
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The effect of selected potential inhibitors of anion transport mediated by the Band 3 protein of the erythrocyte membrane was studied by the electron spin resonance (ESR) technique using Tempo-phosphate spin probe. No inhibition of Band 3-mediated transport by 1-cyano-4-hydroxycinnamic acid, inhibitor of monocarboxylate transporters (MCT) was found but inhibition by some polyphenols (curcumin >...
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متن کاملThe interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane.
Previous studies point to the acidic amino-terminal segment of band 3, the anion transport protein of the red cell, as the common binding site for hemoglobin and several of the glycolytic enzymes to the erythrocyte membrane. We now report on the interaction of hemoglobin with the synthetic peptide AcM-E-E-L-Q-D-D-Y-E-D-E, corresponding to the first 11 residues of band 3, and with the entire 43,...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1981
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.78.5.2898