hemagglutinin/soya

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Accumulation and Subcellular Localization of alpha-Galactosidase-Hemagglutinin in Developing Soybean Cotyledons.

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Ingia / Ingia

We have investigated the accumulation and intracellular localization of soybean (Glycine max [L.] Merr. cv Forrest) alpha-galactosidase-hemagglutinin during seed development. Cotyledon tissue was embedded in Lowicryl K4M and immunocytochemical localization was accomplished through treating thin

Examination of Le and lele Genotypes of Glycine max (L.) Merr. for Membrane-Bound and Buffer-Soluble Soybean Lectin.

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Ingia / Ingia

Membrane fractions from seedlings of four soybean [Glycine max (L.) Merr.] lines were examined by radioimmunoassay and hemagglutination assay for the 120,000 dalton soybean lectin. Two of the lines (Sooty and T-102) are genotypically lele and lack buffer-soluble soybean lectin; the remaining two

Cloning, expression and characterization of a blood group B active recombinant alpha-D-galactosidase from soybean (Glycine max).

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Ingia / Ingia

A cDNA encoding soybean alpha-D-galactosidase [E.C. 3.2.1.22] was obtained by screening a soybean library with Phaseolus alpha-D-galactosidase cDNA. The Glycine max alpha-D-galactosidase cDNA is 1.75 kb long and contains untranslated 5' and 3' sequences. The deduced amino acid sequence of the

An alpha-Galactosidase with Hemagglutinin Properties from Soybean Seeds.

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Ingia / Ingia

Soybean (Glycine max L.) seeds contain a galactose-binding protein which displays two activities: (a) an alpha-galactosidase activity and (b) a hemagglutinin activity. The alpha-galactosidase-hemagglutinin was purified to homogeneity by conventional protein purification procedures and also by

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