Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-1-21
pubmed:abstractText
We demonstrate in vitro the occurrence of a specific but low-affinity interaction between soluble tetrameric rgp160 or soluble monomeric or tetrameric rgp120 and heparin-agarose (HA). This interaction is saturable, pH and temperature-dependent, and can be inhibited by soluble heparin, but not by soluble dextran. In buffer supplemented with 10 mM CaCl2, the C50 of soluble heparin, i.e., the concentration of soluble heparin which leads to 50% inhibition of the binding of [125I]rgp160 or of [125I]rgp120 to HA, is 1.1 x 10(-4) disaccharidic molar concentration for rgp160 and 3.2 x 10(-4) dissacharidic molar concentration for rgp120, which indicates low-affinity interactions. Upon chromatography on HA, [125I]rgp160 is repeatedly eluted as a retarded fraction when compared to the elution volume of [125I]rgp160-soluble heparin complex. Under the same experimental conditions, [125I]rgp120 is also eluted, but as a less retarded fraction than [125I]rgp160. Taken together, these results suggest that, at least part of the described anti HIV-1 activity of heparin might be mediated by interaction with HIV-1 major envelope glycoprotein.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
1180
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The interaction of a glycosaminoglycan, heparin, with HIV-1 major envelope glycoprotein.
pubmed:affiliation
Laboratoire de Biologie cellulaire, Faculté de Médecine Paris-Nord, Bobigny, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't