Species specificity in mouse glycophorin

89, 65, 46 and 29 Kd mouse glycophorin proteins identified during polyacrylamide gel electrophoresis of mouse erythrocytes have been further characterized. These proteins (1) stained positive with Periodic Acid Schiff reagent after sodium hydroxide treatment; (2) labeled using [ 125I] in intact cell...

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Veröffentlicht in:Biochemical and biophysical research communications 1991-04, Vol.176 (2), p.820-825
Hauptverfasser: Wilson, Donella Joyce, Planas, Jose Miguel
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Planas, Jose Miguel
description 89, 65, 46 and 29 Kd mouse glycophorin proteins identified during polyacrylamide gel electrophoresis of mouse erythrocytes have been further characterized. These proteins (1) stained positive with Periodic Acid Schiff reagent after sodium hydroxide treatment; (2) labeled using [ 125I] in intact cells; (3) co-isolated along with integral membrane proteins in the pellet fraction of sodium hydroxide treated ghosts; and (4) demonstrated a molecular weight downshift after neuraminidase treatment during electrophoresis. We have called them mouse Sialoglycoproteins 1,2,3 and 4. Immuno-blot analysis revealed distinct species specificity between human and mouse erythrocyte ghosts, and some cross-reactivity between rat and mouse erythrocyte ghosts.
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subjects Analytical, structural and metabolic biochemistry
Animals
Antibodies - immunology
Biological and medical sciences
Cross Reactions
Electrophoresis, Polyacrylamide Gel
Erythrocyte Membrane - ultrastructure
Fundamental and applied biological sciences. Psychology
glycophorin
Glycophorin - immunology
Glycoproteins
Humans
membrane proteins
Mice
Molecular Weight
Periodic Acid-Schiff Reaction
Proteins
Rats
Species Specificity
title Species specificity in mouse glycophorin
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