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- W2042614251 abstract "A lectin was extracted from Parkia javanica beans and purified by chromatography. The purified lectin showed two forms of proteins, one major and one faint band, both in non-denaturing PAGE and SDS-PAGE. Both of them appeared to be single polypeptide chains with Mr, determined by SDS-PAGE, of 47900 and 45700. The purified lectin could agglutinate red blood cells of rabbit (68267 unit mg−1 protein) and rat (267 unit mg−1 protein), but could not agglutinate red cells of human, sheep or goose. Its hemagglutinating activity was completely inhibited by methyl-α-D-mannosamine and mannose at 5 mM. Ca2+, Mn2+ and Mg2+, but neither EDTA nor EGTA, were effective activators of the purified lectin. The K0.5 of Ca2+, Mn2+ and Mg2+ was 5,17 and 13 mM, respectively. The optimal pH for hemagglutination was 7. The purified lectin was stable in pH 7–10 but labile at temperatures over 50°." @default.
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- W2042614251 date "1995-01-01" @default.
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- W2042614251 title "Purification of a lectin from Parkia javanica beans" @default.
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- W2042614251 doi "https://doi.org/10.1016/0031-9422(94)00550-d" @default.
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