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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-2-3
|
| pubmed:databankReference | |
| pubmed:abstractText |
Biochemical 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Staphylococcal Protein A
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
433-40
|
| pubmed:dateRevised |
2005-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9417100-Amino Acid Sequence,
pubmed-meshheading:9417100-Animals,
pubmed-meshheading:9417100-Base Sequence,
pubmed-meshheading:9417100-Brain,
pubmed-meshheading:9417100-CHO Cells,
pubmed-meshheading:9417100-Carbohydrate Metabolism,
pubmed-meshheading:9417100-Carbohydrates,
pubmed-meshheading:9417100-Catalysis,
pubmed-meshheading:9417100-Cloning, Molecular,
pubmed-meshheading:9417100-Cricetinae,
pubmed-meshheading:9417100-DNA, Complementary,
pubmed-meshheading:9417100-Galactosyltransferases,
pubmed-meshheading:9417100-Humans,
pubmed-meshheading:9417100-Kinetics,
pubmed-meshheading:9417100-Melanoma,
pubmed-meshheading:9417100-Molecular Sequence Data,
pubmed-meshheading:9417100-Recombinant Fusion Proteins,
pubmed-meshheading:9417100-Sequence Homology, Amino Acid,
pubmed-meshheading:9417100-Staphylococcal Protein A
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase catalyzing the formation of type 1 chains.
|
| pubmed:affiliation |
Novartis Pharma AG, Transplantation Preclinical Research, CH 4002 Basel, Switzerland.
|
| pubmed:publicationType |
Journal Article
|