Linked Life Data

3384017

Source:http://linkedlifedata.com/resource/pubmed/id/3384017

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-8-9
pubmed:abstractText
The rod photoreceptor outer segment maintains a remarkable morphology. Two of the proteins which have been implicated in the maintenance of this structure are the 240 kDa spectrin-like protein, and the 220 kDa glycoprotein often referred to as the rim protein. We have probed rat rod outer segment proteins with light-activated (azido-labeled) radioactive nucleotides and found a nucleotide binding site(s) on the rim protein which has a preference for guanine nucleotides. Binding to this site is stimulated by the divalent cations zinc, manganese and magnesium, but not calcium. This site is under investigation and may play a role in stabilizing protein structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
647-55
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Nucleotide binding to the rod outer segment rim protein.
pubmed:affiliation
Jules Stein Eye Institute, University of California, Los Angeles 90024.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.