Studies on Chicken Liver Lectin

概要

論文の詳細を見る
A lectin highly reactive with dermatan sulfate (DS-lectin) was purified from adult chicken liver using new affinity adsorbents which were prepared by immobilizing dermatan sulfate or heparin at the reducing ends on hydrazino-Toyopearl. The DS-lectin behaved as a single protein with a molecular weight of approx. 180,000 by gel chromatography, but could be further dissociated into three proteins with apparent molecular weights of 40,000, 47,000 and 87,000 on SDS polyacrylamide gel electrophoresis. On excitation at 280nm, the DS-lectin emitted fluorescence centered at 336nm, which was attributable to tryptophan residues and could be quenched by the addition of specific saccharides. The association constants of the DS-lectin with specific saccharides were calculated from changes in intensities of fluorescence-difference spectra induced by the saccharides. Dermatan sulfate and protuberic acid, which is composed of L-iduronic acid and D-glucuronic acid (1:2), had the highest association constants among polysaccharides tested. Partially N-desulfated heparin had a higher association constant than that of native heparin while dextran sulfate had no affinity. D-Glucuronic acid and N-acetylneuraminic acid induced weak but significant quenching, but not N-acetylgalactosamine or cellobiose. These results were essentially in agreement with those of hemagglutination inhibition tests and indicated that DS-lectin has a strong affinity for L-iduronic acid residues and probably carboxyl groups in the saccharides, while sulfate groups on the saccharides interfere with the specific interaction.
お茶の水女子大学の論文

Studies on Chicken Liver Lectin

スポンサーリンク

概要

著者

関連論文

スポンサーリンク