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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
22
|
| pubmed:dateCreated |
1998-7-1
|
| pubmed:databankReference | |
| pubmed:abstractText |
Lactosylceramide synthase is an enzyme that catalyzes the transfer of galactose from UDP-Gal to glucosylceramide, and thus participates in the biosynthesis of most glycosphingolipids in mammals. We purified this enzyme over 61,000-fold to near homogeneity with a 29. 7% yield from rat brain membrane fractions. The isolation procedure included solubilization with Triton X-100, affinity chromatography on wheat germ agglutinin-agarose and UDP-hexanolamine-agarose, and hydroxylapatite column chromatography, followed by ion exchange chromatography. The final preparation migrated as a broad band with an apparent molecular mass of 61 kDa on SDS-polyacrylamide gel electrophoresis. This apparent molecular mass was reduced to 51 kDa by N-glycanase digestion, suggesting that the enzyme has a glycoprotein nature. The enzyme required Mn2+ for its activity, and glucosylceramide was its preferred substrate. The cDNA for the enzyme was cloned from a rat brain cDNA library. The cDNA insert encoded a polypeptide of 382 amino acid residues, with a molecular weight of 44,776. The polypeptide contained eight putative glycosylation sites and a 20-amino acid residue transmembrane domain at its N terminus. Amino acid sequence homology analysis revealed that this enzyme shared 39% homology with mouse beta-1, 4-galactosyltransferase (EC 2.4.1.38), which catalyzes the transfer of Gal to beta-1,4-GlcNAc in glycoproteins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
13570-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9593693-Amino Acid Sequence,
pubmed-meshheading:9593693-Animals,
pubmed-meshheading:9593693-Baculoviridae,
pubmed-meshheading:9593693-Base Sequence,
pubmed-meshheading:9593693-Brain,
pubmed-meshheading:9593693-Cell Line,
pubmed-meshheading:9593693-Chromatography, Affinity,
pubmed-meshheading:9593693-Chromatography, Gel,
pubmed-meshheading:9593693-Cloning, Molecular,
pubmed-meshheading:9593693-DNA, Complementary,
pubmed-meshheading:9593693-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9593693-Female,
pubmed-meshheading:9593693-Galactosyltransferases,
pubmed-meshheading:9593693-Male,
pubmed-meshheading:9593693-Mice,
pubmed-meshheading:9593693-Molecular Sequence Data,
pubmed-meshheading:9593693-Rats,
pubmed-meshheading:9593693-Rats, Wistar,
pubmed-meshheading:9593693-Sequence Homology, Amino Acid,
pubmed-meshheading:9593693-Spodoptera
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide beta-1,4-galactosyltransferase from rat brain.
|
| pubmed:affiliation |
Biological Science Laboratories, Kao Corporation, 2606, Akabane, Ichikaimachi, Haga, Tochigi 321-3497, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|