Linked Life Data

2679888

Source:http://linkedlifedata.com/resource/pubmed/id/2679888

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-12-4
pubmed:abstractText
Aldo-keto reductase has been purified 13,000-fold from the lens of the camel (Camelus dromedarius) to a specific activity of 85 U/mg protein. The enzyme is a monomeric protein, exhibiting a Mr = 40,000 upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Camel lens aldo-keto reductase shows a broad substrate specificity, which is strictly dependent on NADPH, and is insensitive to inhibition by Sorbinil and valproate. Aldoses with a carbon chain with more than four residues, as well as glucuronate, are not reduced by the enzyme. On the basis of substrate specificity and sensitivity to inhibition, camel lens aldo-keto reductase appears to be distinct from the so far described aldose, aldehyde and carbonyl reductases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
993
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
116-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Lens aldo-keto reductase of Camelus dromedarius: purification and properties.
pubmed:affiliation
Department of Physiology and Biochemistry, University of Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't