Linked Life Data

37902

Source:http://linkedlifedata.com/resource/pubmed/id/37902

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-10-17
pubmed:abstractText
1. Proteoliposomes containing cytochrome c oxidase and phospholipid have been made by sonication and by the cholate dialysis procedure. In both methods of preparation, only about 50% of the enzyme molecules are oriented in the membrane with their cytochrome c reaction sites exposed to the outside of the vesicle. 2. The activity of cytochrome c oxidase in the reconstituted vesicles in not increased by incubation in 1% Tween 80. Experiments on reconstituted vesicles containing internal (entrapped) cytochrome c indicate that turnover of enzyme oxidising entrapped cytochrome c in the presence of N,N,N',N'-tetramethyl-p-phenylenediamine or 2,3,5,6-tetramethyl-p-phenylendediamine is at a very much lower rate than enzyme oxidising external ferrocytochrome c. 3. Oxidation of ascorbate by externally added cytochrome c results in an electrogenic production of OH- inside the vesicles, which can be monitored using entrapped phenol red. Polylysine inhibits, but does not abolish, the internal alkalinity change in reconstituted vesicles oxidising internal (entrapped) cytochrome c using externably added ascorbate plus N,N,N',N'-tetramethyl-p-phenylenediamine. When 2,3,5,6-tetramethyl-p-phenylenediamine is used as the permeable redox mediator, an increase in internal acidity can be monitored under the same conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
547
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36-46
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Turnover and vectorial properties of cytochrome c oxidase in reconstituted vesicles.
pubmed:publicationType
Journal Article