Linked Life Data

7628468

Source:http://linkedlifedata.com/resource/pubmed/id/7628468

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-9-1
pubmed:abstractText
Glucose-6-phosphate dehydrogenase is inactivated slowly by reaction with sugars (glycation), a process thought to be important in the development of diabetic complications. A major protein from the ocular lens, alpha-crystallin. which exhibits some chaperone-like properties, protects against this inactivation. The well-known molecular chaperone GroEL (chaperonin 60 from Escherichia coli) also protects. On a molar basis, alpha-crystallin is better than GroEL at protecting against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. The relative amounts of enzyme/chaperone indicate that each molecule of alpha-crystallin binds two molecules of the damaged enzyme. This supports the view that alpha-crystallin has a chaperone-like structure as well as a chaperone-like function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
231
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase.
pubmed:affiliation
Nuffield Laboratory of Ophthalmology, University of Oxford, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't