Linked Life Data

9226546

Source:http://linkedlifedata.com/resource/pubmed/id/9226546

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9-10
pubmed:dateCreated
1997-9-16
pubmed:abstractText
The effects of chlorpromazine on the mobility of cytochrome P-450 and the fluidity of lipid membranes have been investigated in bovine adrenocortical submitochondrial particles (SMP). Rotational diffusion of the cytochrome was measured by observing the decay of absorption anisotropy, ra(t), after photolysis of the heme.CO complex by a vertically polarized laser flash. Analysis of ra(t) was based on a 'rotation-about-membrane-normal' model. The anisotropy decayed within 2 ms to a time independent value r3. The presence of chlorpromazine decreased the mobile population of cytochrome P-450 from 28 to 23%. The rotational relaxation time phi a of the mobile population (approximately 1100 microseconds) was, however, not significantly changed by chlorpromazine. The lipid fluidity was examined by observing time-resolved fluorescence anisotropy, rf(t), of 1,6-diphenyl 1,3,5-hexatriene (DPH). The anisotropy rf(t) decayed within 70 ns to a time independent value r infinity. The motion of DPH was analyzed based on a 'wobbling-in-cone' model. The presence of chlorpromazine decreased the cone angle from 42 degrees to 39 degrees, while the rotational relaxation time phi f (approximately 2 ns) was not significantly changed by the presence of chlorpromazine. These results demonstrate that chlorpromazine decreased the mobility of not only lipids but also membrane proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0731-7085
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1215-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Time resolved study of effect of chlorpromazine on mobility of cytochrome P-450 and phospholipids in the inner membrane of adrenocortical mitochondria.
pubmed:affiliation
Department of Biophysics and Life Science, Graduate School of Arts and Sciences, University of Tokyo at Komaba, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't