Isolation and properties of beta-galactoside binding lectins of calf heart and lung.

摘要: A soluble lectin which agglutinates trypsin-treated rabbit erythrocytes was purified from calf heart using affinity chromatography on asialofetuin-Sepharose. Its molecular weight determined by gel filtration to be approximately 17,000. On polyacrylamide electrophoresis in sodium dodecyl sulfate, the predominant species had a of 9,000, suggesting that is dimer. Binding studies performed with iodinated revealed neuraminidase-treated contained 5 X 10(6) binding sites per cell. Native and bound lectin, but human rat required neuraminidase trypsin treatment, respectively, for occur. number saccharides, glycopeptides, glycoproteins possess haptene inhibitory activity toward erythrocytes. The most potent these have either galactose beta leads to, N-acetylglucosamine or sequences at their nonreducing termini. Lactose 1 3N-acetylgalactosamine are next best haptenes. Finally, alpha-linked residues free very weak presences terminal sialic acid residue impairs all instances. Calf also contains membrane-associated similar not identical lectin. beta-galactoside isolated lung. It has same size subunit structure as antigenically identical. In studies, pattern inhibition various haptenes three lectins.