ISOLATION AND CHARACTERIZATION OF CAJANUS-CAJAN LECTIN

Cajanus cajan lectin was isolated by ammonium sulfate fractionation and affinity chromatography on an IgM-Sepharose 6B column. Gel filtration and SDS-PAGE showed size homogeneity of the lectin. The lectin with M(r) 18,000 on SDS-PAGE had gel filtration behavior which was consistent with a molecular weight of 39 kDa and a Stokes radius of 2.74 nm. The results showed that the lectin is a dimer composed of identical subunits with N- and C-terminal residues of threonine and alanine, respectively. The glycoprotein lectin contained 3% concanavalin A-reactive neutral carbohydrates. Its amino acid composition is characterized by high contents of acidic amino acids. The number of tyrosine and tryptophan residues per mole of the lectin was determined to be 14 and 4, respectively, by spectrophotometry. Results on the effects of large numbers of saccharides on lectin-mediated hemagglutination and lectin-IgM precipitation showed that the C. cajan lectin was specific for mannose and glucose. A comparative study of the properties of C. cajan lectin and concanavalin also presented. (C) 1995 Academic Press, Inc.