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| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C0009017 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C0311878 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9506957 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9506957 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:9506957 | pubmed:dateCreated | 1998-4-16 | lld:pubmed |
| pubmed-article:9506957 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9506957 | pubmed:abstractText | We isolated a cDNA encoding a novel glucuronyltransferase from human placenta cDNA with the use of the degenerate reverse transcriptase-polymerase chain reaction method. Degenerate primers were designed based upon the amino acid sequence alignment of rat glucuronyltransferase (GlcAT-P) involved in the biosynthesis of the carbohydrate epitope HNK-1 with putative proteins in Caenorhabditis elegans and Schistosoma mansoni. The new cDNA sequence revealed an open reading frame coding for a protein of 335 amino acids with a type II transmembrane protein topology. The amino acid sequence displayed 43% identity to the rat GlcAT-P, and the highest sequence identity was found in the COOH-terminal catalytic domain. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active glucuronyltransferase with marked specificity for a glycoserine Galbeta1-3Galbeta1-4Xylbeta1-O-Ser. In contrast, asialoorosomucoid, which contains the Galbeta1-4GlcNAc sequence and is a good acceptor substrate for the GlcAT-P, did not serve as an acceptor. The reaction product was sensitive to beta-glucuronidase digestion and co-chromatographed with authentic GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser in high-performance liquid chromatography, suggesting that the enzyme is a beta1, 3-glucuronyltransferase. These results indicate that this new member of the glucuronyltransferase gene family is the enzyme previously described as glucuronyltransferase I that forms the glycosaminoglycan-protein linkage region, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, of proteoglycans. | lld:pubmed |
| pubmed-article:9506957 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9506957 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9506957 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9506957 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9506957 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9506957 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:OgawaTT | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:OkaSS | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:KitagawaHH | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:KawasakiTT | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:SugaharaKK | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:TamuraJJ | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:TonkSS | lld:pubmed |
| pubmed-article:9506957 | pubmed:author | pubmed-author:NeumannK WKW | lld:pubmed |
| pubmed-article:9506957 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9506957 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:9506957 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9506957 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9506957 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9506957 | pubmed:pagination | 6615-8 | lld:pubmed |
| pubmed-article:9506957 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9506957 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9506957 | pubmed:articleTitle | Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. | lld:pubmed |
| pubmed-article:9506957 | pubmed:affiliation | Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 658, Japan. | lld:pubmed |
| pubmed-article:9506957 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9506957 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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