Source:http://linkedlifedata.com/resource/pubmed/id/20959391
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2011-2-7
|
pubmed:abstractText |
We previously identified two novel enzymes in pigeon, ?1,4- and ?1,4-galactosyltransferases (GalTs), which are responsible for the biosynthesis of the Gal?1-4Gal and Gal?1-4Gal sequences on glycoproteins, respectively. No such glycan structures and/or enzymes have been found in mammals, suggesting that the expression of these enzymes diverged during the course of vertebrate evolution. To compare their expression profiles among avian species, we first established a method for detecting the activities of these two GalTs based on the two-dimensional high pressure liquid chromatography mapping technique, using 2-aminopyridine-derivatized asialo-biantennary N-glycans as an acceptor substrate. When we analyzed the activities of GalTs in pigeon liver extracts in the presence of UDP-Gal, 13 different products containing Gal?1-4Gal?1-4GlcNAc, Gal?1-4Gal?1-4GlcNAc and/or Gal?1-4Gal?1-4Gal?1-4GlcNAc branches were identified. The newly formed glycosidic linkages of the enzymatic products were determined by nuclear magnetic resonance and methylation analysis, as well as by galactosidase digestions. The activities of both ?1,4- and ?1,4-GalTs were detected in various tissues in pigeon, although their relative activities were different in each tissue. In contrast, ostrich expressed ?1,4-GalT, but not ?1,4-GalT, in all tissues analyzed, whereas neither ?1,4- nor ?1,4-GalT activity was detected in chicken. These results indicate that ?1,4- and ?1,4-GalTs are expressed in a species-specific manner and are distributed throughout the entire body of pigeon or ostrich when the enzymes are present.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
1460-2423
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
21
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
283-94
|
pubmed:meshHeading |
pubmed-meshheading:20959391-Animals,
pubmed-meshheading:20959391-Cations, Divalent,
pubmed-meshheading:20959391-Chickens,
pubmed-meshheading:20959391-Columbidae,
pubmed-meshheading:20959391-Enzyme Assays,
pubmed-meshheading:20959391-Female,
pubmed-meshheading:20959391-Galactosyltransferases,
pubmed-meshheading:20959391-Glycoproteins,
pubmed-meshheading:20959391-Hydrogen-Ion Concentration,
pubmed-meshheading:20959391-Liver,
pubmed-meshheading:20959391-Organ Specificity,
pubmed-meshheading:20959391-Polysaccharides,
pubmed-meshheading:20959391-Species Specificity,
pubmed-meshheading:20959391-Struthioniformes
|
pubmed:year |
2011
|
pubmed:articleTitle |
Distinct expression profiles of UDP-galactose: ?-D-galactoside ?1,4-galactosyltransferase and UDP-galactose: ?-D-galactoside ?1,4-galactosyltransferase in pigeon, ostrich and chicken.
|
pubmed:affiliation |
Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan. nrsuzuki@k.u-tokyo.ac.jp
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|