pubmed-article:12626393 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0560175 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C1882857 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0006556 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C1706209 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0560013 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:12626393 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:12626393 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:12626393 | pubmed:dateCreated | 2003-4-18 | lld:pubmed |
pubmed-article:12626393 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:abstractText | A rat intestinal beta1,6N-acetylglucosaminyltransferase (beta1-6GnT) responsible for the formation of the beta1,6-branched poly-N-acetyllactosamine structure has been purified to apparent homogeneity by successive column chromatographic procedures using an assay wherein pyridylaminated lacto- N-triose II (GlcNAcbeta1-3Galbeta1-4Glc-PA) was used as an acceptor substrate and the reaction product was GlcNAcbeta1-3(GlcNAcbeta1-6)Galbeta1-4Glc-PA. The purified enzyme catalyzed the conversion of the polylactosamine acceptor GlcNAcbeta1-3'LacNAc into GlcNAcbeta1-3'(GlcNAcbeta1-6') LacNAc (dIGnT activity), but it could not transfer GlcNAc to LacNAcbeta1-3'LacNAc (cIGnT activity). This enzyme could also convert mucin core 1 and core 3 analogs, Galbeta1-3GalNAcalpha1-O-paranitrophenyl (pNP) and GlcNAcbeta1-3GalNAcalpha1-O-pNP, into Galbeta1-3(GlcNAcbeta1-6) GalNAcalpha1-O-pNP (C2GnT activity) and GlcNAcbeta1-3(GlcNAcbeta1-6)GalNAcalpha1-O-pNP (C4GnT activity), respectively. Based on the partial amino acid sequences of the purified protein, the cDNA encoding this enzyme was cloned. The COS-1 cells transiently transfected with this cDNA had high dI/C2/C4GnT activities in a ratio of 0.34:1.00:0.90, compared with non- or mock-transfected cells. The primary structure shows a significant homology with human and viral mucin-type core 2 beta1-6GnTs (C2GnT-Ms), indicating that this enzyme is the rat ortholog of human and viral C2GnT-Ms. This is the first identification and purification of this enzyme as a major carrier of dIGnT activity in the small intestine. This rat ortholog should mostly be responsible for making distal I-branch structures on poly-N-acetyllactosamine sequences in this tissue, as well as making mucin core 2 and core 4 structures, given that it also has high C2/C4GnT activities. | lld:pubmed |
pubmed-article:12626393 | pubmed:language | eng | lld:pubmed |
pubmed-article:12626393 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12626393 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12626393 | pubmed:month | May | lld:pubmed |
pubmed-article:12626393 | pubmed:issn | 0959-6658 | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:HonkeKoichiK | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:TaniguchiNaoy... | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:TakioKojiK | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:DohmaeNaoshiN | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:TaguchiTomohi... | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:SakamotoYoshi... | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:RenkonenOssiO | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:HelinJariJ | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:ToivonenSuviS | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:SalminenHeidi... | lld:pubmed |
pubmed-article:12626393 | pubmed:author | pubmed-author:KorekaneHiroa... | lld:pubmed |
pubmed-article:12626393 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12626393 | pubmed:volume | 13 | lld:pubmed |
pubmed-article:12626393 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12626393 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12626393 | pubmed:pagination | 387-400 | lld:pubmed |
pubmed-article:12626393 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:meshHeading | pubmed-meshheading:12626393... | lld:pubmed |
pubmed-article:12626393 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12626393 | pubmed:articleTitle | Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1-4Glc(NAc)-R [GlcNAc to Gal]beta1,6N-acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine. | lld:pubmed |
pubmed-article:12626393 | pubmed:affiliation | Department of Biochemistry, Osaka University Medical School/graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan. | lld:pubmed |
pubmed-article:12626393 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12626393 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:12626393 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:286976 | entrezgene:pubmed | pubmed-article:12626393 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12626393 | lld:entrezgene |