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Immunochemical Studies of Lectins
Author(s) -
Miller J. T.,
Boyd W. C.
Publication year - 1967
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1967.tb03390.x
Subject(s) - lectin , sephadex , staining , chemistry , biochemistry , chromatography , affinity chromatography , size exclusion chromatography , phytohemagglutinins , microbiology and biotechnology , biology , immunology , enzyme , immune system , t cell , lymphocyte activation , genetics
Summary A method for the partial purification of Sophora japonica lectin is described. Tests on the partially purified lectin showed it to possess an increased specific activity for A and B erythrocytes but to have a low activity for group O erythrocytes. Chromatographic analysis on G‐200 sephadex showed two distinct peaks for the purified lectin and only one for the crude lectin, suggesting that partly purified lectin had a slightly smaller molecular size than did the crude material. Differences were also found between crude lectin and partly purified lectin by electrophoretic analysis and DEAE cellulose chromatography employing bromphenol blue staining of the protein and erythrocyte staining to locate the hemagglutinating activity.