AI Article Synopsis
- Glycophorin A (GPA) is a key sialoglycoprotein found in red blood cell membranes, extracted from blood groups A, B, and O using phenol-water methods.
- Differences in interactions between GPA samples and three specific lectins (PVL, WGA, SNA-I) were studied through surface plasmon resonance (SPR) analysis, revealing that desialylated GPA samples show weaker reactions compared to native samples.
- The study concluded that SPR is an effective technique for studying glycoprotein and lectin interactions, which could help identify variations in carbohydrate components across different glycoprotein samples.
Article Abstract
Glycophorin A (GPA), the major sialoglycoprotein of the human erythrocyte membrane, was isolated from erythrocytes of healthy individuals of blood groups A, B and O using phenol-water extraction of erythrocyte membranes. Interaction of individual GPA samples with three lectins (Psathyrella velutina lectin, PVL; Triticum vulgaris lectin, WGA and Sambucus nigra I agglutinin SNA-I) was analyzed using a BIAcore biosensor equipped with a surface plasmon resonance (SPR) detector. The experiments showed no substantial differences in the interaction between native and desialylated GPA samples originating from erythrocytes of either blood group and each of the lectins. Desialylated samples reacted weaker than the native ones with all three lectins. PVL reacted about 50-fold more strongly than WGA which, similar to PVL, recognizes GlcNAc and Neu5Ac residues. SNA-I lectin, recognizing alpha2-6 linked Neu5Ac residues, showed relatively weak reaction with native and only residual reaction with desialylated GPA samples. The data obtained show that SPR is a valuable method to determine interaction of glycoproteins with lectins, which potentially can be used to detect differences in the carbohydrate moiety of individual glycoprotein samples.
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