Abstract
89, 65, 46 and 29 Kd mouse glycophorin proteins identified during polyacrylamide electrophoresis of mouse erythrocytes have been further characterized. These proteins (1) stain 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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