| pubmed-article:2730922 | pubmed:abstractText | Lectin activity has been detected in the thigh muscle extracts of Rana tigerina, which was found to agglutinate both trypsinized and untrypsinized rabbit erythrocytes. The lectin has been purified to homogeneity by MEPBS (0.01 M phosphate-buffered saline (pH 7.2) with 4 mM beta-mercaptoethanol) buffer extraction of the tissue and affinity chromatography on acid-treated Sepharose 6B. The molecular weight (Mr) of the purified lectin was determined by SDS-polyacrylamide gel electrophoresis and gel filtration on Sephadex G-75, which gave values of 15,500 +/- 1000 and 32,000 +/- 1000, respectively, suggesting that the lectin is a dimer. Amino acid composition data of the lectin has revealed that it contains a high proportion of glycine and alanine, and low amounts of sulphur-containing amino acids. Hapten-inhibition study of this lectin has shown that it is galactose-specific. Hemagglutination activity of the lectin can also be inhibited by beta-galactoside containing oligosaccharides. | lld:pubmed |
