Linked Life Data

8077855

Source:http://linkedlifedata.com/resource/pubmed/id/8077855

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-10-3
pubmed:abstractText
The in vitro activity of sialyltransferase IV (SAT-IV), which catalyzes the transfer of sialic acid to the terminal galactose of different gangliotetraosylceramides (GA1, GM1a and GD1b), was examined in membrane-enriched preparations from mouse embryos at embryonic day 12 (E-12). Gangliosides GD1a and GT1b were the only reaction products using GM1a and GD1b as substrates, respectively. The Km values for GM1a and GD1b were 53 microM and 42 microM, respectively. Competitive inhibition experiments showed that the same enzyme (SAT-IV) catalyzed sialic acid transfer to the terminal galactose residues of both GM1a and GD1b. Two labeled ganglioside products were obtained, however, using GA1 as a substrate. One product was identified as ganglioside GM1b and the enzymatic reaction for its formation was maximal at pH 6.0, similar to that for GD1a and GT1b formation. The second product, synthesized by a different sialyltransferase, was identified as GD1 alpha based on results from TLC immunostaining, neuraminidase digestion, and periodate oxidation-borohydride reduction. The pH dependence curve for GD1 alpha formation had a different shape than that for GM1b formation with a maximum at pH 6.3. GD1 alpha is apparently synthesized from GM1b by an endosialyltransferase that catalyzes the transfer of a second sialic acid to the internal N-acetylgalactosamine of GM1b. The formation of both GM1b and GD1 alpha was linear over protein concentration. The ratio of GD1 alpha/GM1b formation varied from 0.25 to 1.20 depending on the GA1 substrate concentration.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
993-1001
pubmed:dateRevised
2008-8-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Ganglioside biosynthesis in mouse embryos: sialyltransferase IV and the asialo pathway.
pubmed:affiliation
Department of Biology, Boston College, Chestnut Hill, MA 02167.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't