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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1986-11-24
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pubmed:abstractText |
Cells of B16 mouse melanoma grown in serum-free medium in the presence of [3H]glucosamine secreted or shed labeled glycoproteins. A wheat germ agglutinin-binding glycoprotein was isolated that accounted for 37% of the total [3H]glucosamine incorporated; it had a molecular weight of approximately 50,000 and was absent in less-tumorgenic wheat germ agglutinin (isolectin I)-resistant variants of the cells. The glycoprotein contained approximately 25% of serine and threonine plus equimolar amounts of glucosamine and galactosamine, indicating both N- and O-linked oligosaccharide chains. Neuraminidase treatment released approximately 60% of the glycoprotein's 3H radioactivity as N-acetylneuraminic acid. The sialoglycoprotein did not, but the desialylated species did, bind (97%) to ricin-Sepharose, suggesting the presence of terminal sialic acid and penultimate galactose residues in most of the saccharide units. Alkaline borohydride released 61% of the glycoprotein's radioactivity as oligosaccharide alcohols that were mainly tetrasaccharides (75%) with some branched trisaccharides (10%) from the O-linked structures. Hydrazinolysis and analysis of the alkaline borohydride-resistant portion of the glycoprotein indicated the presence of mainly triantennary, complex-type structures (N-linked) containing three sialic acids residues plus L-fucose. Serial lectin-affinity chromatography of the hydrazine-released saccharides with concanavalin A-agarose, pea lectin-agarose, L-PHA-agarose, and E-PHA-agarose, indicated the absence of high-mannose or hybrid-type structures and further confirmed the presence of triantennary, complex-type units.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylneuraminic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mitogen,
http://linkedlifedata.com/resource/pubmed/chemical/Sialic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Wheat Germ Agglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/wheat germ agglutinin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0008-6215
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
151
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-64
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3768903-Animals,
pubmed-meshheading:3768903-Cell Line,
pubmed-meshheading:3768903-Glucosamine,
pubmed-meshheading:3768903-Glycoproteins,
pubmed-meshheading:3768903-Melanoma, Experimental,
pubmed-meshheading:3768903-Mice,
pubmed-meshheading:3768903-Molecular Weight,
pubmed-meshheading:3768903-N-Acetylneuraminic Acid,
pubmed-meshheading:3768903-Oligosaccharides,
pubmed-meshheading:3768903-Receptors, Mitogen,
pubmed-meshheading:3768903-Sialic Acids,
pubmed-meshheading:3768903-Tritium,
pubmed-meshheading:3768903-Wheat Germ Agglutinins
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pubmed:year |
1986
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pubmed:articleTitle |
Isolation and characterization of a wheat germ agglutinin-binding glycoprotein from B16 mouse melanoma cells.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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