favin/broad bean

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The chemical characterization of favin, a lectin isolated from Vicia faba.

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We have determined the subunit structure of the glucose- and mannose-binding lectin favin, from Vicia faba. The molecule is composed of two nonidentical polypeptide chains held together by noncovalent interactions. We have determined the complete amino acid sequence of the smaller alpha chain (Mr =

Amino acid sequence and variant forms of favin, a lectin from Vicia faba.

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We have determined the complete amino acid sequence (182 residues) of the beta chain of favin, the glucose-binding lectin from fava beans (Vicia faba), and have established that the carbohydrate moiety is attached to Asn 168. Together with the sequence of the alpha chain previously reported

In vitro translation and processing of a precursor form of favin, a lectin from Vicia faba.

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Favin, the glucose- and mannose-binding lectin isolated from fava (Vicia faba) beans, consists of two polypeptide chains (alpha, Mr = 5,571; beta, Mr = 20,700). Translation of fava bean mRNA in vitro in a wheat germ-derived system yields a single favin polypeptide chain of Mr = 29,000. This molecule

Favin, a crystalline lectin from Vicia faba.

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Properties of α-galactosidase II(2) from Vicia faba seeds.

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α-Galactosidase II(2) (MW ∼ 43 390) from resting Vicia faba L. seeds had been shown to possess D-glucose/D-mannose-specific lectin activity. Inhibition studies with monosaccharides and an examination of the effects of heat and pH on the catalytic and lectin activities of the enzyme indicate that the

Three-dimensional structure of favin: saccharide binding-cyclic permutation in leguminous lectins.

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The three-dimensional structure of favin, the glucose- and mannose-binding lectin of Vicia faba (vetch, broad bean), has been determined at a resolution of 2.8 angstroms by molecular replacement. The crystals contain specifically bound glucose and provide the first high-resolution view of specific

Binding and degradation of lectins by components of rumen liquor.

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The binding of 15 different plant lectins to feed particles and microbes in rumen liquor, and their degradation were studied in vitro. The rate of degradation assessed from the label released when radioactive iodine-labelled lectins were incubated with rumen liquor conflicted with the rates

Identification of cysteine proteases and screening of cysteine protease inhibitors in biological samples by a two-dimensional gel system of zymography and reverse zymography.

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We have developed a two-dimensional (2D-) gel system of zymography and reverse zymography for the detection and characterization of proteases and protease inhibitors. Isoelectric focusing (IEF) agarose gels with pH gradients were employed for separation in the first-dimension and sodium dodecyl

Characterization and antimicrobial activity of lectins purified from three Egyptian leguminous seeds.

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Lectins are carbohydrate-binding proteins that play vital roles in many biological processes. In this study, lectins from three Egyptian cultivars (fava bean, lentil, and pea) were isolated by precipitation with different concentrations of ammonium sulfate. The purification process was performed by

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