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J. Biochem, 1982, Vol. 91, No. 4 1139-1146
© 1982 Japanese Biochemical Society

research-article

Purification and Characterization of a Lectin from the Shellfish, Saxidomus purpuratus

Masahiro TATSUMI, Yuji ARAI and Tatsuro ITOH

Institute of Applied Biochemistry, The University of Tsukuba Niihari-gun, Ibaraki 305

A lectin was purified from a shellfish, Saxidomus purpurarus, using ion-exchange chromatography on DEAE-cellulose and affinity chromatography on N-acetylglucosamine-Sepharose. The lectin purified by affinity chromatography showed seven protein bands in polyacrylamide gel electrophoresis. The two major lectins (SPA-I and SPA-IT!) were purified by a second DEAE-cellulose column chromatography. The molecular weights of the lectins were almost the same and were estimated to be around 40,000 by gel filtration on a Sepharose 6B column. On SDS-polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol, the lectins showed molecular weights of 14,000. The isoelectric points of SPA-I and -III were estimated to be 4.4 and 4.1, respectively. The two lectins (SPA-I and -In) differed slightly in amino acid composition and were glycoproteins containing 2.1 and 3.8 mol of GIcNAc per 40,000 g of the lectin, respectively. The binding constant of SPA-I or SPA-rn for methyl N-acetyl-a-D-glucosaminide, the strongest inhibitor of hemagglutination in this experiment, was estimated to be 1.3 x 103 or 4.2 x I04 M–1, respectively, by the UV difference spectroscopy method.


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