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- W2043443321 abstract "Abstract The affinity purified Sophora japoniea lectin exhibits an anomalous behavior on polyacrylamide gel electrophoresis (PAGE). Electrophoresis at pH 8.9 produces three protein staining bands. Extraction and re-electrophoresis of the fastest and slowest migrating components demonstrates that the lectin solution is an equilibrium mixture of interconvertible forms. Addition of a bindable saccharide, D-galactose, during PAGE causes the equilibrium to be shifted toward a single form. As indicated by analytical gel filtration, sedimentation velocity ultracentrifugation and ion-exchange chromatography experiments, the equilibrium mixture consists of charge and not molecular weight variants of the native molecule of 132,800 g/m. Results from end-group and cysteine analyses and PAGE in sodium dodecyl sulfate indicate that the native lectin is composed of the non-covalent association of two dissimilar subunits. One subunit consists of two identical polypeptide chains attached by two disulfide bonds and the other subunit of two identical polypeptide chains stabilized by a single cysteine bridge." @default.
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- W2043443321 date "1980-01-01" @default.
- W2043443321 modified "2023-09-27" @default.
- W2043443321 title "Properties and Subunit Characterization of Affinity Purified Sophora Japonica Lectin" @default.
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- W2043443321 doi "https://doi.org/10.1080/00327488008061733" @default.
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