Studies on lectins. LVIII. Sugar-binding properties, as determined by affinity electrophoresis, of alpha-D-galactosidases from Vicia faba seeds possessing erythroagglutinating activity |
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Authors: | P Maly M Tichá J Kocourek |
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Abstract: | The interaction of alpha-D-galactosidases from Vicia faba seeds with saccharides was studied by means of affinity electrophoresis on polyacrylamide gel in an acidic buffer system. For the preparation of affinity gels, water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used. alpha-D-Galactosidases interact with immobilized O-alpha-D-galactosyl residues and glycogen, but no interaction was observed with immobilized O-alpha-D-mannosyl residues. On the basis of the results of affinity electrophoresis performed in the presence of various free sugars, dissociation constants of the various alpha-D-galactosidase-free sugar complexes were calculated. |
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