Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-4-29
pubmed:abstractText
The naturally occurring dithiols DL-dihydrolipoate and DL-dihydrolipoamide were tested for their ability in the removal of ferritin-bound iron. Both compounds remove the iron stored inside the protein by complexing it in the ferric form. The iron can be reduced to the ferrous form by excess dithiol, but this is not necessary for complete removal. Reaction is complete in few hours and, at molar ratios of chelator to metal higher than 10, more than 60% of the ferritin-bound iron was removed. The amount of iron stored in the ferritin molecule does not affect the rate and the yield of the removal reaction. The iron-removing ability of DL-dihydrolipoate was found to be identical to that of an equimolar solution of sodium dithionite, and to be pH-dependent. Results are discussed in terms of the molecular architecture of ferritin and of the chelators, and their possible physiological relevance is pointed out.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
155
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-300
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Removal of ferritin-bound iron by DL-dihydrolipoate and DL-dihydrolipoamide.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't