文章基本信息

标题：Three Rhamnose-Binding Lectins from Osmerus eperlanus mordax (Olive Rainbow Smelt) Roe
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作者：Masahiro HOSONO ; Hiroaki KAWAUCHI ; Kazuo NITTA 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：1993
卷号：16
期号：3
页码：239-243
DOI：10.1248/bpb.16.239
出版社：The Pharmaceutical Society of Japan
摘要：Three rhamnose-binding lectins were purified from the roe of Osmerus eperlanus mordax (olive rainbow smelt) by affinity chromatography and ion-exchange chromatography. The apparent molecular weights of Osmerus eperlanus mordax lectin (OML) -1, -2 and -3 were 25000, 32000 and 26000, respectively, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. On native PAGE, these three lectins showed different migration patterns (Rm value; 0.37, 0.53 and 0.66, respectively). OMLs agglutinated rabbit and human type B erythrocytes and sarcoma 180 cells, but not human type A and O erythrocytes and AH109A cells. The most effective monosaccharide inhibitor was L-rhamnose. L-Mannose and D-galactose were also good inhibitors. Furthermore, OML-induced hemagglutination was inhibited more strongly by melibiose or raffinose rather than lactose or lactulose. Therefore, OMLs are L-rhamnose/α-D-galactosyl type lectins. OMLs did not require a detergent, when extracted from crude material, and Ca²⁺, Mg²⁺, EDTA and dithiothreitol were not necessary for the OML-induced hemagglutination activities. The OMLs had similar N-terminal amino acid sequences.
关键词：rhamnose-binding lectin;fish roe;N-terminal sequence;affinity chromatography