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• W2005067315 abstract "Abstract The surface membrane glycoproteins of normal mouse erythrocytes can be labeled by oxidation with either periodate or galactose oxidase in the presence of neuraminidase, followed by reduction with NaB3H4. Without neuraminidase there is little galactose oxidase-catalyzed labeling of protein. Analysis of labeled proteins by SDS-polyacrylamide gel electrophoresis showed that both methods labeled the same set of glycoproteins. Plasmodium berghei infection dramatically reduced the sialoglycoprotein labeling of red blood cells from infected blood using the periodate/NaB3H4 method. Provided neuraminidase was present, labeling by the galactose oxidase method gave identical results to normal erythrocytes. We conclude that the glycoprotein sialic acid of uninfected as well as infected red cells is modified during infection such that it is refractory to periodate oxidation. Acylation of the exocyclic hydroxyls of sialic acid is suggested to account for this. Lectin binding and cell agglutination experiments using Limulin, soybean and wheatgerm lectins, and concanavalin A confirmed and extended these observations. The possible implications of these results with regard to anemia induced by malaria are briefly discussed." @default.
• W2005067315 created "2016-06-24" @default.
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• W2005067315 date "1981-02-01" @default.
• W2005067315 modified "2023-09-26" @default.
• W2005067315 title "Plasmodium berghei: Modification of sialic acid on red cells from infected mouse blood" @default.
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• W2005067315 doi "https://doi.org/10.1016/0014-4894(81)90046-1" @default.
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