Linked Life Data

9417100

Source:http://linkedlifedata.com/resource/pubmed/id/9417100

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pubmed-article:9417100pubmed:abstractTextBiochemical evidence suggests that the galactosyltransferase activity synthesizing type 1 carbohydrate chains is separate from the well characterized enzyme that is responsible for the synthesis of type 2 chains. This was recently confirmed by the cloning, from melanoma cells, of an enzyme capable of synthesizing type 1 chains, which was shown to have no homology to other galactosyltransferases. We report here the molecular cloning and functional expression of a second human beta3-galactosyltransferase distinct from the melanoma enzyme. The new beta3-galactosyltransferase has homology to the melanoma enzyme in the putative catalytic domain, but has longer cytoplasmic and stem regions and a carboxyl-terminal extension. Northern blots showed that the new gene is present primarily in brain and heart. When transfected into mammalian cells, this gene directs the synthesis of type 1 chains as determined by a monoclonal antibody specific for sialyl Lewisa. A soluble version of the cloned enzyme was expressed in insect cells and purified. The soluble enzyme readily catalyzes the transfer of galactose to GlcNAc to form Gal(beta1-3)GlcNAc. It also has a minor but distinct transfer activity toward Gal, LacNAc, and lactose, but is inactive toward GalNAc.lld:pubmed
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pubmed-article:9417100pubmed:dateRevised2005-11-17lld:pubmed
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pubmed-article:9417100pubmed:year1998lld:pubmed
pubmed-article:9417100pubmed:articleTitleCloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase catalyzing the formation of type 1 chains.lld:pubmed
pubmed-article:9417100pubmed:affiliationNovartis Pharma AG, Transplantation Preclinical Research, CH 4002 Basel, Switzerland.lld:pubmed
pubmed-article:9417100pubmed:publicationTypeJournal Articlelld:pubmed
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