Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2007-11-23
pubmed:abstractText
The beta-casein-derived octapeptide RINKKIEK is a noncompetitive inhibitor of soybean lipoxygenase (LOX). To investigate the molecular determinants for the enzyme-peptide interaction, a peptide library containing substitutional analogs of RINKKIEK was prepared by SPOT synthesis and analyzed for interaction with fluorescent-labeled LOX. The positively charged amino acid residues in RINKKIEK appear to be essential for the LOX-peptide interaction. Replacement of the negatively charged glutamic acid by any other amino acid residue improves LOX binding. For both RINKKIPK and RINKKISK this increase in LOX binding is accompanied by a threefold increase in LOX inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2268-75
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Improvement of lipoxygenase inhibition by octapeptides.
pubmed:affiliation
Laboratory of Biochemistry, Wageningen University, P.O. Box 9101, 6700 HB Wageningen, The Netherlands. marloes.schurink@wur.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't