Linked Life Data

1841544

Source:http://linkedlifedata.com/resource/pubmed/id/1841544

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1992-11-13
pubmed:abstractText
Syntheses of tuftsin-like partial sequences of HIV-1 and HIV-2 gp-120 proteins: Thr-Lys-Ala-Lys (I), Thr-Lys-Ala-Lys-Arg (II), Pro-Thr-Lys-Ala-Lys-Arg (III), Thr-Lys-Glu-Lys (IV), Thr-Lys-Glu-Lys-Arg (V), and Pro-Thr-Lys-Glu-Lys-Arg (VI) are described. From HIV-1 partial sequences peptide I inhibited the phagocytosis stimulating activity of tuftsin. The inhibitory potency diminished progressively for peptides II and III, in parallel to the increase of their slight phagocytosis stimulating activity. Similar results were obtained also for the fragments of the HIV-2 gp120 protein. The inhibitory activity, clearly visible for IV, diminished with peptide chain elongation. Peptides IV and VI were devoided of the phagocytosis stimulating activity while peptide V was slightly active.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0004-069X
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
469-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Competition between tuftsin and HIV-1, HIV-2 envelope protein sequences.
pubmed:affiliation
Institute of Chemistry, Wroc?aw University.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't