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oligosaccharide a/phaseolus
Veza se sprema u međuspremnik
3 rezultati
Complex-type glycoproteins synthesized in the subcommissural organ of mammals. Light- and electron-microscopic investigations by use of lectins.
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The secretory activity in the subcommissural organ (SCO) of the sheep and cow was examined by means of lectin histochemistry and cytochemistry. Among the various lectins tested. Concanavalin A (Con A) revealed glycoproteins rich in mannosyl residues in the rough endoplasmic reticulum of ependymal
Effect of carbohydrate and metal ion binding on the reactivity of the essential thiol groups of lima bean lectin.
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A free sulfhydryl group previously has been shown to be required for carbohydrate binding to the lectin from lima bean (Phaseolus lunatus) (Gould, N. R. and Scheinberg, S. L. (1970) Arch. Biochem. Biophys. 141, 607-613). Modification of this group by sulfhydryl reagents was specifically inhibited by
Developmental changes in the molecular weights of polypeptides in the human CNS that carry the HNK-1 epitope and bind Phaseolus vulgaris lectins.
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The binding patterns of electrophoresed polypeptides from homogenates of human frontal lobe, cerebellum, and spinal cord obtained at various stages of development were determined for several lectins with specificities for a wide range of oligosaccharides. A discrete developmental change in the
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