Linked Life Data

739988

Source:http://linkedlifedata.com/resource/pubmed/id/739988

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1979-4-28
pubmed:abstractText
The effect of modification of photoreceptor membranes of the bovine retina on the termodynamical parameters that characterize heat denaturation of rodopsin was studied. The highest increase of the rate constant and the corresponding maximal drop of the free energy change of heat denaturation of the pigment were obtained by using 7 M urea or 25% Triton X-100 in the presence of 5.10(-4) M EDTA. After chipping off one third of the protein from the rodopsin molecule by papain treatment a significant decrease of the slope of the Arrenius curve and a maximal decrease of entropy change compared to the parameters known for heat denaturation of the pigment in native photoreceptor membranes were found. Modification of the lipid components of the photoreceptor membranes (treatment with Triton X-100 and phospholipase C) reduced the thermostability of rodopsin. Maximal changes were obtained at Triton X-100 concentrations 0.1--1%, further concentration increas (1--25%) did not lead to significant changes. Phospholipase C treatment resulted in a decrease of free energy change and an increase of entropy change without affecting entalpy changes, accompaning the heat denaturation of rodopsin. Bivalent cations (Ca2+, Mg2+) increased the termostability of rodopsin both in photoreceptor membranes and in solutions to 25% Triton X-100.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1012-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
[Modification of the retina photoreceptor membranes and temperature stability of rhodopsin].
pubmed:publicationType
Journal Article, English Abstract