Linked Life Data

3561501

Source:http://linkedlifedata.com/resource/pubmed/id/3561501

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6113
pubmed:dateCreated
1987-5-11
pubmed:abstractText
The major components of mammalian lenses are tissue-specific, soluble proteins, the alpha-, beta- and gamma-crystallins. The lenses of other vertebrate classes often contain other major proteins, notably delta-crystallin in birds and reptiles. A fourth distinct type, described as epsilon-crystallin, is prominent in many bird and crocodile lenses. Here we show that epsilon-crystallin is an active glycolytic enzyme, lactate dehydrogenase (LDH) (EC 1.1.1.27) and that duck epsilon-crystallin appears to be identical to duck LDH-B4. LDH is a normal metabolic component in other lenses, but in duck is present in amounts far exceeding the requirements of any likely catalytic role. It appears that an active enzyme has been recruited, unchanged, to an extra role as a structural protein in the lens without gene duplication and sequence divergence. This surprising discovery raises the possibility that other crystallins may similarly be enzymes expressed at high levels in lens as structural proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
326
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
622-4
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't