The purification of wheat-germ agglutinin by precipitation with ammonium sulphate and by chromatography on Sephadex G-75, Sepharose-ovomucoid and CM-cellulose is described. This procedure gave agglutinin preparations which were homogeneous on polyacrylamide gels under a variety of conditions. Purified wheat-germ agglutinin formed colourless solutions and was relatively insoluble at neutral pH; ...

The glycoproteins of plasma membranes from axenically grown Dictyostelium discoideum and human red blood cells (O+) were characterized according to their apparent molecular weights in sodium dodecyl sulfate-polyacrylamide gels and their ability to bind lectins. This was achieved by diffusing each of several fluorescein-conjugated lectins into sodium dodecyl sulfate-polyacrylamide gels which con...

Fernitin-conjugated plant lectins of varying sacchanide specificities were used to characterize oligosacchanides present on the surface of mouse mammary tumor virus (MMTV) produced in cells of mammary tumors of mice of C3H/He/Tex, A/Dm, and RlII/Dm strains. Mouse mammary tumor (MMT) cells grown on discs of FEP Teflon were labeled in situ with fennitin conjugates of concanavalin A specific for a...

The combined application of thin-section and critical-point-drying "fracture-label" is used to determine the pattern of distribution and partition of wheat-germ agglutinin and concanavalin A binding sites on the membrane faces of freeze-fractured exocrine and endocrine rat pancreatic cells. Whereas the exoplasmic face of plasma membrane is preferentially labeled by both lectins, the endoplasmic...

The binding of iodinated wheat germ agglutinin, Ricinus communis agglutinin, and concanavalin A to mycoplasma cells and membranes was examined. All mycoplasmas studied specifically bound concanavalin A or R. communis agglutinin and, to a lesser degree, wheat germ agglutinin. The binding of lectins to whole cells was similar to that recorded for membranes, suggesting that significant binding on...

We used thin-section fracture-label to determine the distribution of wheat-germ agglutinin binding sites in intracellular membranes of secretory and nonsecretory rat tissues as well as in human leukocytes. In all cases, analysis of the distribution of wheat germ agglutinin led to the definition of two endomembrane compartments: one, characterized by absence of the label, includes the membranes ...

A lectin slide agglutination test has been developed for the confirmatory identification of Neisseria gonorrhoeae. With wheat germ lectin as an agglutinin, 164 of 165 clinical isolates of N. gonorrhoeae gave a 3 to 4+ reaction within 6 to 8 min. Four gonococcal isolates, even though negative by the fluoresecent-antibody method, gave strong positive reactions with the wheat germ lectin. Among 23...

Wheat germ agglutinin is a hevein class N-Acetylglucosamine–binding protein with specific toxicity and biomedical potential. It extractable from wheat germ—a low-value byproduct of the industry—using well–established extraction methods based on salt precipitation affinity chromatography. Due to its N-Acetylglucosamine affinity, exhibits antifungal properties as well cytotoxic properties. Its an...

of human erythrocyte ghosts were solubilized with 0.5yc Triton X-100 in 56 mM sodium borate, pH 8.0. This procedure solubilized 51% of the membrane protein, 81% of the sialic acid, 89% of the receptors for the Agaricus bisporus lectin and 70 to 75% of the wheat germ agglutinin and Ricinus communis lectin receptors. The solubilized glycoproteins were then separated by affinity chromatography on ...