Linked Life Data

16662812

Source:http://linkedlifedata.com/resource/pubmed/id/16662812

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-6-29
pubmed:abstractText
Purified aconitase, an iron-sulfur protein, from either beef heart mitochondria or pig heart can be activated fully by light when combined with washed thylakoid membranes from pea (Pisum sativum L.) chloroplasts. The light activation of the enzyme does not require any other additive or cofactor and is sensitive to 3-(3,4-dichlorophenyl)-1,1-dimethyl urea, 2,6-dichlorophenol-indophenol, ferricyanide, and methyl viologen, indicating that the photoelectron transport system of the thylakoid membranes, and in particular, photosystem I, is involved in the process of activation. Light activation of the enzyme is also markedly inhibited when the thylakoid membranes are treated with sulfite or arsenite, and abolished totally when the membranes are treated with Zwittergent, suggesting that the light effect mediator involved in the light modulation of chloroplastic enzymes mediates the activation of purified aconitase also.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Feb
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-50
pubmed:dateRevised
2010-9-14
pubmed:year
1983
pubmed:articleTitle
Light Activation of Purified Aconitase by Washed Thylakoid Membranes of Pea (Pisum sativum L.).
pubmed:affiliation
Department of Biological Sciences, University of Illinois at Chicago, Box 4348, Chicago, IL 60680.
pubmed:publicationType
Journal Article