Linked Life Data

6375671

Source:http://linkedlifedata.com/resource/pubmed/id/6375671

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-7-20
pubmed:abstractText
The titration by ferrocyanide and the localization of the oxidizing equivalents of lactoperoxidase "compound II" were studied as a function of pH. It was demonstrated that 1) whatever the pH, the structure of lactoperoxidase "compound II" was compatible with a Fe IV R degree state, 2) at acidic pH, ferrocyanide preferentially reduced the oxidizing equivalent localized on the heme iron to give an Fe III R degree compound, 3) at pH 4.2 only the Fe III R degree form was obtained after reduction of lactoperoxidase "compound II" with one mole of ferrocyanide and whereas at pH greater than 4.2, a mixture of both Fe III R degree and Fe IV R forms was present, 4) lowering the pH from 7.2 to 4.0 induced a transition of Fe IV R state to Fe III R degree state, but increasing the pH from 4.0 to 7.2 did not permit the formation of Fe IV R compound from Fe III R degree compound.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
121
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
463-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Reduction of lactoperoxidase-H2O2 compounds by ferrocyanide: indirect evidence of an apoprotein site for one of the two oxidizing equivalents.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't