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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1997-4-17
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pubmed:abstractText |
Lectin blot analysis of bovine, goat, human, rabbit and mouse serum immunoglobulin G (IgG) samples revealed that Wisteria floribunda agglutinin (WFA) binds to the heavy chains of bovine, goat and human serum IgG proteins but not those of the rabbit and mouse proteins. WFA-positive light chain bands were also detected in bovine, goat and human serum IgG samples only after the filters were treated with Arthrobacter ureafaciens sialidase. The WFA-binding to these IgG proteins was abolished by treatment of the filter with sialidase and then beta-N-acetylhexosaminidase or N-glycanase prior to incubation with the lectin. WFA-agarose column chromatography of the oligosaccharides released by hydrazinolysis from the IgG samples followed by reduction with NaB3H4 revealed that 0.15, 0.09 and 0.07% of the total oligosaccharides from bovine, goat and human serum IgG samples bind to the column, respectively. Partial characterization of WFA-positive bovine IgG oligosaccharides by Bio-Gel P-4 column chromatography suggested that the major oligosaccharide is of non-fucosylated biantennary complex-type. These results indicate that beta-N-acetylgalactosaminylation occurs to N-linked sugar chains of heavy and light chains of IgG proteins in a species-specific manner.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Hexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetyl-Galactosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/wisteria lectin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
1334
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9101715-Animals,
pubmed-meshheading:9101715-Blotting, Western,
pubmed-meshheading:9101715-Cattle,
pubmed-meshheading:9101715-Goats,
pubmed-meshheading:9101715-Hexosaminidases,
pubmed-meshheading:9101715-Humans,
pubmed-meshheading:9101715-Immunoglobulin G,
pubmed-meshheading:9101715-Lectins,
pubmed-meshheading:9101715-Mice,
pubmed-meshheading:9101715-Plant Lectins,
pubmed-meshheading:9101715-Rabbits,
pubmed-meshheading:9101715-Receptors, N-Acetylglucosamine,
pubmed-meshheading:9101715-Species Specificity,
pubmed-meshheading:9101715-beta-N-Acetyl-Galactosaminidase
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pubmed:year |
1997
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pubmed:articleTitle |
Species-specific beta-N-acetylgalactosaminylation of serum IgG proteins.
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pubmed:affiliation |
Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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