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http://purl.uniprot.org/citations/8611500http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8611500http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8611500http://www.w3.org/2000/01/rdf-schema#comment"Sialyltransferase activities, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), in Colo 205 cells catalyze the transfer of sialic acid to the terminal galactose of GlcNc-- and GalNAc-containing glycolipid substrates, respectively. Competition kinetic studies with nLcOse4Cer and GM1 as substrates in a sialyltransferase assay show that these two activities are catalyzed by two different catalytic entities. The two enzymes were co-solubilized with taurochlorate and resolved by DEAE--Cibacron Blue--Sepharose column chromatography into two elution peaks. The column eluent with SAT-3 activity failed to transfer sialic acid to asialo alpha(1)-acid glycoprotein, indicating that this enzyme is different from the sialyltransferase (ST3N) that synthesizes NeuAc alpha 2-3Gal linkage in asparagine-linked oligosaccharides of glycoprotein. However, SAT-3 activity can be immunoprecipitated with a polyclonal antibody produced against a protein expressed in Escherichia coli as GST-fusion protein from an ECB cDNA homolog of an alpha 2-3 sialyltransferase SAT-3 or STZ) the has been cloned from human melanoma cell and human placenta. Thus a concentration-dependent decrease in the residual SAT-3 activity relative to SAT-4 activity was observed in the supernatant after precipitation of the immune complex. Expression of SAT-3 (STZ) cDNA was also detected in Colo 205 cell by RT-PCR, followed by sequence analysis of the RT-PCR product. Characterization of the catalytic reaction products of SAT-3 and SAT-4 with thin-layer chromatography, sialidase treatment, and binding to specific antibodies indicates that both SAT-3 and SAT-4 catalyze the formation of alpha 2-3 linkage between sialic acid and terminal galactose of glycolipid substrates."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.org/dc/terms/identifier"doi:10.1021/bi960239l"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.org/dc/terms/identifier"doi:10.1021/bi960239l"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu S."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu S."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu S.S."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu S.S."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu M."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/author"Basu M."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/pages"5166-5174"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/pages"5166-5174"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/title"Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/title"Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line."xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/8611500http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/8611500http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8611500
http://purl.uniprot.org/citations/8611500http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8611500
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