| pubmed-article:1820200 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1820200 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1820200 | lifeskim:mentions | umls-concept:C0521454 | lld:lifeskim |
| pubmed-article:1820200 | lifeskim:mentions | umls-concept:C0017953 | lld:lifeskim |
| pubmed-article:1820200 | lifeskim:mentions | umls-concept:C0877853 | lld:lifeskim |
| pubmed-article:1820200 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:1820200 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1820200 | pubmed:dateCreated | 1992-8-3 | lld:pubmed |
| pubmed-article:1820200 | pubmed:abstractText | Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively. Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy. The results are summarized as follows: (i) oligosaccharides attached to Asn-52 of hCG alpha comprised monosialylated 'monoantenary' NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3[Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N1-4'), disialylated diantennary NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3[NeuAc alpha 2-3-Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N2), and the monosialylated hybrid-type structures NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3[Man alpha 1-3Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N1-A) and NeuAc alpha 2-3Gal-beta 1-4GlcNAc beta 1-2Man alpha 1-3[Man alpha 1-3(Man alpha 1-6)Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N1-AB) in a ratio approaching 5:2:2:1; (ii) Asn-78 of hCG alpha carried N2 and N1-4' almost exclusively (ratio approximately 3:2); (iii) both N-glycosylation sites of hCG beta contained predominantly component N2, partially (approximately 25%) and completely alpha 1-6-fucosylated at the N-acetylglucosamine linked to Asn-13 and Asn-30, respectively. The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase. | lld:pubmed |
| pubmed-article:1820200 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1820200 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1820200 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1820200 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1820200 | pubmed:issn | 0959-6658 | lld:pubmed |
| pubmed-article:1820200 | pubmed:author | pubmed-author:RenwickA GAG | lld:pubmed |
| pubmed-article:1820200 | pubmed:author | pubmed-author:WeisshaarGG | lld:pubmed |
| pubmed-article:1820200 | pubmed:author | pubmed-author:HiyamaJJ | lld:pubmed |
| pubmed-article:1820200 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1820200 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:1820200 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1820200 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1820200 | pubmed:pagination | 393-404 | lld:pubmed |
| pubmed-article:1820200 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
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| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:meshHeading | pubmed-meshheading:1820200-... | lld:pubmed |
| pubmed-article:1820200 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1820200 | pubmed:articleTitle | Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. | lld:pubmed |
| pubmed-article:1820200 | pubmed:affiliation | Department of Biochemistry, University of Auckland, New Zealand. | lld:pubmed |
| pubmed-article:1820200 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1820200 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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