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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3 Pt 1
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pubmed:dateCreated |
1988-10-17
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pubmed:abstractText |
Human glycosylated alpha-amylase contains a single biantennary N-linked oligosaccharide that terminates with the structure Fuc alpha 1,3(Gal beta 1,4)GlcNAc. To examine the role of terminal fucose in the clearance of alpha-amylase, we used lectin affinity chromatography to isolate an alpha-amylase fraction that contains two terminal fucoses (one in each branch of the oligosaccharide) and a fraction from which both terminal fucoses have been enzymatically removed. In the rat, the rate of clearance of the radioiodinated fraction with terminal fucoses is rapid (t1/2 = 12 min) and is slowed by mannosylated but not galactosylated bovine serum albumin. The rate of clearance of the radioiodinated alpha-amylase fraction with no terminal fucoses is also rapid (t1/2 = 9.5 min), but the clearance is now slowed by galactosylated bovine serum albumin. These findings indicate that the fucosylated and defucosylated alpha-amylase fractions are recognized by different carbohydrate-specific receptors. We conclude therefore that terminal fucose is the recognition marker that effects the physiological clearance of this glycoprotein.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
255
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G374-81
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3262312-Carbohydrate Conformation,
pubmed-meshheading:3262312-Carbohydrate Sequence,
pubmed-meshheading:3262312-Chromatography, Affinity,
pubmed-meshheading:3262312-Fucose,
pubmed-meshheading:3262312-Humans,
pubmed-meshheading:3262312-Molecular Sequence Data,
pubmed-meshheading:3262312-Saliva,
pubmed-meshheading:3262312-alpha-Amylases,
pubmed-meshheading:3262312-alpha-L-Fucosidase
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pubmed:year |
1988
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pubmed:articleTitle |
Role of terminal fucose residues in clearance of human glycosylated alpha-amylase.
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pubmed:affiliation |
Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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