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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1983-10-8
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pubmed:abstractText |
We have previously reported the enzymatic synthesis of galactosyl-beta 1,3-N-acetylglucosamine using membrane preparations from pig trachea (Sheares, B. T., Lau, J. T. Y., and Carlson, D. M. (1982) J. Biol. Chem. 257, 599-602). The enzyme catalyzing the synthesis of this disaccharide, UDP-galactose:N-acetylglucosamine 3 beta-galactosyltransferase, has been solubilized and contaminating galactosyltransferases, including the UDP-galactose:N-acetylglucosamine 4 beta-galactosyltransferase and the UDP-galactose:N-acetylgalactosamine-mucin 3 beta-galactosyltransferase, were removed by affinity chromatography on alpha-lactalbumin-agarose, N-acetylglucosamine-agarose, and asialo-ovine submaxillary mucin bound to DEAE-Sephacel. UDP-galactose:N-acetylglucosamine 3 beta-galactosyltransferase and a yet unidentified UDP-galactose:N-acetylglucosamine 4 beta-galactosyltransferase, both not retained by the alpha-lactalbumin-agarose, were further purified by adsorption to a UDP-hexanolamine-Sepharose column and these two galactosyltransferase activities were finally resolved by gel filtration on Sephacryl S-200. The purified UDP-galactose:N-acetylglucosamine 3 beta-galactosyltransferase displays an absolute requirement for a divalent cation (Mn2+ or Co2+) and is most active at pH 6.0. Unlike the UDP-galactose:N-acetylglucosamine 4 beta-galactosyltransferase, UDP-galactose:N-acetylglucosamine 3 beta-galactosyltransferase is not inhibited by high concentrations of N-acetylglucosamine. Apparent Km values are UDP-galactose, 0.23 mM, and N-acetylglucosamine, 385 mM. The apparent Km for a synthetic acceptor, N-acetylglucosaminyl-beta 1, 3-N-acetylgalactosamine-O-benzyl, was 2.4 mM. Acceptor specificity suggests that this 3 beta-galactosyltransferase is responsible for elongation of oligosaccharide chains in mucin glycoproteins and in glycolipids.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cobalt,
http://linkedlifedata.com/resource/pubmed/chemical/Lactose Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetyllactosamine Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nickel
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9893-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6411707-Animals,
pubmed-meshheading:6411707-Chromatography, Affinity,
pubmed-meshheading:6411707-Chromatography, Gel,
pubmed-meshheading:6411707-Cobalt,
pubmed-meshheading:6411707-Hydrogen-Ion Concentration,
pubmed-meshheading:6411707-Lactose Synthase,
pubmed-meshheading:6411707-Manganese,
pubmed-meshheading:6411707-Mucins,
pubmed-meshheading:6411707-N-Acetyllactosamine Synthase,
pubmed-meshheading:6411707-Nickel,
pubmed-meshheading:6411707-Swine,
pubmed-meshheading:6411707-Trachea
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pubmed:year |
1983
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pubmed:articleTitle |
Characterization of UDP-galactose:2-acetamido-2-deoxy-D-glucose 3 beta-galactosyltransferase from pig trachea.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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