Comparative Studies of Carbohydrate-Binding Proteins from Xenopus laevis Skin and Eggs : Sugar-Binding Specificities and Affinity Purification

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Salt and detergent extracts of acetone-dried powder of Xenopus laevis skin and eggs were fractionated on sugar-Sepharose columns, to which lactose, melibiose, galactose, rhamnose and mannose had been covalently linked, by successive elution with chelating reagent and specific sugars, resulting in separation of the different Ca^<2+> -dependent and Ca^<2+> -independent carbohydrate-binding proteins. The skin of X. laevis contains a salt-extractable Ca^<2+> -dependent lactose-binding lectin of 30 kilodalton (kDa) and the eggs a similar lectin of 43kDa, but they both lack Ca^<2+> -dependent galactose-binding lectins, The 30 kDa lactose-binding lectin which agglutinates human A erythrocytes was isolated by successive affinity chromatography on two linked sugar-Sepharose columns, i.e., a galactose-Sepharose-lactose-Sepharose (GL) column system. Since the 30 kDa lectin was not recovered in the Ca^<2+> -dependent lactose-binding protein fraction from the GL column system under the dithiothreitol (DTT)-free conditions, it was concluded that the lectin requires the presence of DTT and calcium for binding to the lactose-Sepharose column.
公益社団法人日本薬学会の論文
1990-04-25