onobrychis viciifolia/cysteine

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Lectin from sainfoin (Onobrychis viciifolia scop.). Complete amino acid sequence.

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The complete amino acid sequence of a lectin from sainfoin ( Onobrychis viciifolia Scop . var. Eski ) has been determined by sequential Edman analyses of the intact protein and peptides derived from digests with trypsin and thermolysin. Peptides were purified by pH fractionation, by gel filtration,

Isolation and properties of a lectin from sainfoin (Onobrychis viciifolia, Scop.).

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A glycoprotein capable of binding simple carbohydrates and causing hemagglutination has been isolated from seeds of the legume plant sainfoin (Onobrychis viciifolia, Scop. var Eski). The phytolectin was prepared by affinity chromatography of pH 7.0 sodium phosphate extracts on columns of

Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannose specific lectins.

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The D-mannose specific lectin from sainfoin was prepared by affinity chromatography on Sephadex G-75, and its circular dichroism (CD), metal content, antigenic character, and N-terminal amino acid sequence were compared with those of four lectins from Vicieae plants and concanavalin A. The sainfoin

The dinitrophenyl group as a selective label in high-performance liquid chromatography of peptides.

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1-Fluoro-2,4-dinitrobenzene can be used to selectively label histidine, tyrosine, and cysteine residues in maleylated proteins. The usefulness of the resulting chromophores for peptide mapping by high-performance liquid chromatography was demonstrated with the lectin from sainfoin (Onobrychis

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