Abstract
A 1000-fold purification of anti-A hemagglutinating lectin from Falcata japonica was obtained by means of ammonium sulfate fractionation, gel filtration of Sephadex G-100 and affinity chromatography on N-acetyl-D-galactosamine-starch. The isolated lectin formed a single diffuse band in polyacrylamide gel electrophoresis and has an approximate molecular weight of 120, 000 as estimated by measurements of Sephadex G-200 gel filtration and ultracentrifugal analysis. The lectin was rich in asparatic acid, serine and glycine. Trace of methionine was detected but no cystine was found.
