Oda Y, Ichida S, Mimura T, Maeda K, Tsujikawa K, Aonuma S
J Pharmacobiodyn. 1984 Sep;7(9):614-23. doi: 10.1248/bpb1978.7.614.
A lectin was isolated from the external mucus of fish, Genypterus blacodes. This is the first lectin isolated from fish. The molecular weight of the lectin, determined by gel filtration, was approximately 32 000, whereas 8 000 was indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Amino acid analysis demonstrated that the lectin contained large amounts (near 30% of the residues) of lysine, but no tryptophan. The lectin agglutinated mouse, rabbit and human erythrocytes at a concentration of 15.6 micrograms/ml. An inhibition test revealed that the lectin was strongly inhibited by N-acetyl-glucosamine, mucin and orosomucoid. Binding studies performed with iodinated asialo-orosomucoid indicated that the lectin contained a high affinity binding site with a dissociation constant of 1.1 X 10(-8) M. The lectin required the presence of calcium ion for both its hemagglutination and binding activity.
从黑口裸盖鱼的外部黏液中分离出一种凝集素。这是首次从鱼类中分离出的凝集素。通过凝胶过滤测定，该凝集素的分子量约为32000，而在2-巯基乙醇存在下进行的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示其分子量为8000。氨基酸分析表明，该凝集素含有大量（近30%的残基）赖氨酸，但不含色氨酸。该凝集素在浓度为15.6微克/毫升时可凝集小鼠、兔和人的红细胞。抑制试验表明，N-乙酰葡糖胺、黏蛋白和类黏蛋白可强烈抑制该凝集素。用碘化去唾液酸类黏蛋白进行的结合研究表明，该凝集素含有一个高亲和力结合位点，解离常数为1.1×10⁻⁸M。该凝集素的血细胞凝集和结合活性均需要钙离子的存在。
