Proteolysis of band 3 is enhanced by anti-Rh sub(o)(D) binding to the red cell membrane

Proteolysis of band 3 is enhanced by anti-Rh sub(o)(D) binding to the red cell membrane

Surface radioiodinated human red cells were incubated with IgG fractions and the radioelectrophoretic profile of the ghost membranes determined. The patterns of RH sub(o)(D)-negative membranes exposed to anti-RH sub(o)(D) IgG and Rh sub(o)(D)-positive membranes exposed to non-immune IgG fractions re...

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Veröffentlicht in:Biochemical and biophysical research communications 1984-01, Vol.124 (2), p.437-442
Hauptverfasser: Yictoria, E J, Kleeman, JE, Masouredis, S P
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Sprache:eng
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band 3 protein
erythrocytes
immunoglobulin G
man
proteolysis
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Kleeman, JE
Masouredis, S P
description Surface radioiodinated human red cells were incubated with IgG fractions and the radioelectrophoretic profile of the ghost membranes determined. The patterns of RH sub(o)(D)-negative membranes exposed to anti-RH sub(o)(D) IgG and Rh sub(o)(D)-positive membranes exposed to non-immune IgG fractions remained intact. Membranes of RH sub(o)(D)-positive membranes following incubation with anti-Rh sub(o)(D) IgG showed a sharp reduction in the quantity of intact band 3, the main glycoprotein of the red cell membrane. This was significantly abrogated in the presence of protease inhibitors. The results suggest a possible role for IgG binding in promoting the generation of band 3-derived fragments described by others as normal constituents of isolated ghosts.
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source Elsevier ScienceDirect Journals
subjects band 3 protein
erythrocytes
immunoglobulin G
man
proteolysis
title Proteolysis of band 3 is enhanced by anti-Rh sub(o)(D) binding to the red cell membrane
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