Abstract
Material that interacts with concanavalin A has been purified from seed extracts of 18 species (16 legumes, Coffea arabica and Lolium perenne) by Con A-Sepharose chromatography. When examined by sodium dodecyl sulphate-polyacrylamide disc gel electrophoresis, many of the preparations showed a number of protein-staining components. All the preparations gave a single precipitation line against Cunalialia ensiformis crude extract on gel diffusion plates. Some of the con A-interacting preparations were shown to possess haemagglutination activity. The Arachis hypogaea (peanut) preparation contains one major glycoprotein of molecular weight 69 000, which was further purified and analysed. The purified glycoprotein contains 12% carbohydrate, galactose being the major sugar with minor amounts of mannose and xylose present.
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