Linked Life Data

8240815

Source:http://linkedlifedata.com/resource/pubmed/id/8240815

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-12-23
pubmed:abstractText
Hydrolysis of GTP by the photoreceptor G protein transducin (Gt alpha) was found to occur with kinetics identical to the inactivation of its effector cGMP phosphodiesterase (PDE), but was too slow (tens of seconds) in dilute rod outer segment (ROS) suspensions to account for subsecond recovery of the light response. Raising the concentration of ROS membranes increased the rates of GTP hydrolysis and PDE inactivation in parallel as much as 6-fold. Holo-PDE and its gamma subunit had weak effects on GTPase kinetics (< 1.6-fold and < 1.3-fold, respectively). ROS membranes stripped of PDE retained approximately 90% of a GTPase accelerating activity that was protease sensitive, indicating that they contain a GTPase-accelerating factor distinct from PDE.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
939-49
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes.
pubmed:affiliation
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't