Lectin in egg-mass of fresh water snail,
Biomphalaria glabrata (PR strain), was purified and studied biochemically.
This lectin (
B. glabrata agglutinin, BGA) had agglutination activity against human A type and B type erythrocyte, whereas it did not agglutinate human O type erythrocyte and rabbit erythrocyte. Since this agglutination activity was inhibited most strongly with N-Acetyl-D-glucosamine (GlcNAc) of all the tested saccharides, purification of the BGA was carried out using affinity chromatography with GlcNAc-Sepharose and gel chromatography with Sepharose 4B.
Electrophoresis of 4-15% polyacrylamide gel showed that purified BGA was constituted with two protein components. Either of them had pI 5.1, and their M. W. was roughly estimated to be more than 150, 000.
Moreover, to study polypeptide components of BGA, purified BGA was analyzed using SDS polyacrylamide gel electrophoresis (SDS-PAGE) and O'Farrell's two dimensional gel electrophoresis (2D-PAGE). SDS-PAGE pattern of purified BGA showed one polypeptide band, but two polypeptide spots, one was major and the other was minor, were found in 2D-PAGE pattern. The major polypeptide component of BGA had pI 5.1 and M. W. 18, 200, while minor component had pI 4.9 and the same M. W. as the major one.
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