Isolation of Two Agglutinins with Different Biological Properties from the Eggs of Rana catesbiana

Open Access
Publisher Website
Google Scholar
Abstract
Eggs of R. catesbiana contained 2 agglutinins showing specific reactivities, 1 with human blood group A erythrocytes and the other with mouse Ehrlich ascites carcinoma cells and rat ascites hepatoma cells (AH-109A). These agglutinins were purified by chromatography over Sephadex G-75, DEAE- and CM-cellulose and hydroxyapatite column. The purified anti-A agglutinin contained about 1.6% carbohydrate and the MW estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate was 17,000. The purified cancer cell agglutinin contained about 0.6% carbohydrate and the MW was 15,000. Its electrophoretic mobility on cellulose acetate membrane was similar to that of basic proteins such as protamine and histone. Two agglutinins had similar amino acid compositions, and showed a relatively large amount of glutamic acid and aspartic acid but a small amount of lysine, arginine and histidine. The agglutinating activity of anti-A agglutinin is inhibited by oligosaccharides such as lactose and N-acetyllactosamine, whereas that of cancer cell agglutinin is specifically inhibited only by ganglioside obtained from human blood group A erythrocytes. The remarkable difference in the biological properties of these agglutinins are discussed.