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hemagglutinin/arachide
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Purification and properties of a nonspecific hemagglutinin from the peanut (Arachis hypogaea).
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Systemic and oral immunogenicity of hemagglutinin protein of rinderpest virus expressed by transgenic peanut plants in a mouse model.
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Rinderpest causes a devastating disease, often fatal, in wild and domestic ruminants. It has been eradicated successfully using a live, attenuated vaccine from most part of the world leaving a few foci of disease in parts of Africa, the Middle East, and South Asia. We have developed transgenic
[Some chemical and serological properties of non-dialysable fractions of human seminal plasmas].
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Some chemical and serological properties of water-soluble and undialysable fraction (WSF) and water-insoluble and undialysable fraction (WISF) of human seminal plasmas were studied. Both of the fractions contained proteins as the main components and also carbohydrates as minor components, and each
Carbohydrate chain analysis by lectin binding to electrophoretically separated glycoproteins from murine B16 melanoma sublines of various metastatic properties.
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Cellular glycoprotein carbohydrate chains of B16 melanoma sublines of various metastatic colonization capacities were analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and direct lectin staining, combined with chemical modification of carbohydrate chains in
[Separation of Thomsen-Friedenreich (T) antigen and N antigen precursor glycoproteins from perchloric acid-soluble fraction of cyst fluid of human ovarian clear cell carcinoma and their some chemical and serological properties].
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One M perchloric acid-soluble fraction separated from cyst fluid of a patient (blood group AB) with ovarian clear cell carcinoma in malignant was subjected to Sephacryl S-200 gel filtration and Fraction 1 which was eluted at void volume, reacted with both of the lectins of Vicia unijuga and Arachis
Syntheses of O-beta-D-galactopyranosyl-(1 leads to 3)-0-(2-acetamido-2-deoxy-alpha(and -beta)-D-galactopyranosyl)-N-tosyl-L-serine and their interaction with D-galactose-binding lectins.
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In order to use, as hapten inhibitors against various galactose-binding lectins, the derivatives of O-beta-D-galactopyranosyl-(1 leads to 3)-O-(2-acetamido-2-deoxy-alpha-D-galactopyranosyl)-L-serine, which is the common core structure of sugar chains of most mucins, the synthesis of these compounds
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