Linked Life Data

7999128

Source:http://linkedlifedata.com/resource/pubmed/id/7999128

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-1-17
pubmed:abstractText
The kinetics of acid- and sialidase-catalyzed hydrolysis of the interketosidic linkages of two different disialic acids, Neu5Gc alpha 2-->5-OglycolylNeu5Gc and Neu5Gc alpha 2-->8Neu5Gc, were studied. The former sequence was recently identified in the polysialic acid chains of a sialic acid-rich glycoprotein isolated from the egg jelly coat of two different species of sea urchins, and the latter was previously found in the cortical alveolar-derived polysialoglycoprotein from rainbow trout eggs. At pH values < 3.8, the rate of hydrolysis of Neu5Gc alpha 2-->5-OglycolylNeu5Gc was greater than that of Neu5Gc alpha 2-->8Neu5Gc. Paradoxically, however, Neu5Gc alpha 2-->5-OglycolylNeu5Gc was more stable than Neu5Gc alpha 2-->8Neu5Gc at pH values > 3.8. These findings indicate a greater contribution of intramolecular general acid catalysis to the lability of the alpha 2-->5-ketosidic linkage. Neu5Gc alpha 2-->5-OglycolylNeu5Gc was a poor substrate for Arthrobacter ureafaciens, Clostridium perfringens, and Vibrio cholerae sialidases, in contrast to Neu5Gc alpha 2-->8Neu5Gc. Neu5Gc alpha 2-->5-OglycolylNeu5Gc was essentially resistant to hydrolysis by A. ureafaciens sialidase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
893-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Differential reactivity of two types of N-glycolyneuraminic acid dimers toward enzymatic and nonenzymatic hydrolysis of their interketosidic linkages.
pubmed:affiliation
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't