Linked Life Data

11958645

Source:http://linkedlifedata.com/resource/pubmed/id/11958645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2002-4-17
pubmed:abstractText
The processes of absorption, blood transport, tissular distribution, metabolism, and excretion are at present understood very little. The aim of this study was to investigate blood transport and identify which principal plasma proteins in humans and rats bind to monomeric catechin and procyanidins in red wine ex vivo. Human and rat plasma and serum were incubated with (+)-catechin and procyanidins from grape seed, the origin of red wine catechins. Proteins were separated by SDS-PAGE and native-PAGE to determine which proteins bound to these compounds. The principal protein that bound to (+)-catechin in each species was sequenced. SDS-PAGE showed that (+)-catechin and procyanidins mainly bound to a protein of about 80 kDa in rats and 35 kDa in humans. Their sequencing indicated that these proteins were apo A-I in humans and transferrin in rats. The fact that red wine procyanidins bind to both proteins suggests that they may have a role in reverse cholesterol transport and in the oxidizing action of iron.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2708-12
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Human apo A-I and rat transferrin are the principal plasma proteins that bind wine catechins.
pubmed:affiliation
Departament de Bioquímica i Biotecnologia, CeRTA, Universitat Rovira i Virgili, P. Imperial Tàrraco 1, 43005 Tarragona, Spain.
pubmed:publicationType
Journal Article