Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-1-5
pubmed:abstractText
The rate of GTP hydrolysis in the active site of transducin and that of the release of the phosphate thus formed have been measured. The former step has been found to be a rate-limiting one. The rate constant for GTP hydrolysis is equal to 0.027 s-1 at 23 degrees C, and 0.07 s-1 at 37 degrees C. Besides, it has been shown that the rate of GTPase reaction on the transducin alpha-subunit does not depend on the concentration of a complex of transducin beta- and gamma-subunits or on the presence of cGMP phosphodiesterase and a 48 kDa protein from rod outer segments. According to the results, GTP hydrolysis on transducin proceeds too slowly to account for the rapid quenching of a phosphodiesterase cascade in rod outer segments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
224
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-22
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
On the role of transducin GTPase in the quenching of a phosphodiesterase cascade of vision.
pubmed:affiliation
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
pubmed:publicationType
Journal Article