Abstract
The hemolymph of kuruma prawn Penaeus japonicus agglutinated horse, sheep, chicken, and human erythrocytes, but not a marine bacterium Vibrio anguillarum. The hemagglutinating activity was dependent on the presence of calcium ions. The higher titer values were obtained by keeping the reaction mixture at 6°C for 16 h compared to those observed at room temperature. The hemagglutinating activity was inhibited by glycoproteins and simple sugars such as mucin Type I, mucin Type II, fetuin, D-mannosamine, N-acetyl-D-glucosamine, and N-acetylneuraminic acid. The lectins were purified by affinity chromatography on mucin Type II-Sepharose 6 B. Succeeding separation by ion-exchange chromatography and gel-filtration revealed that the affinity purified lectins were a mixture of the lectins with different molecular species and also sugar-binding specificity. The two lectins were obtained in electrophoretically pure form; one (Fraction B-1) was a protein of 370 kDa consisted of subunits of 84 kDa and the other (Fraction D, 240 kDa) consisted with subunits of 34 kDa.
