Immunological and chemical analysis of P6, the carboxyl-terminal fragment of HIV P15. NLM AIDSLINE Important note: Information in this article was accurate in 1988. The state of the art may have changed since the publication date.

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Immunological and chemical analysis of P6, the carboxyl-terminal fragment of HIV P15.

AIDS Res Hum Retroviruses. 1987 Fall;3(3):253-64. Unique Identifier : AIDSLINE MED/88134682
Veronese FD; Rahman R; Copeland TD; Oroszlan S; Gallo RC; Sarngadharan MG; Bionetics Research, Inc., Rockville, MD 20850.

Abstract: The first open reading frame of the HIV genome has been identified as the gag gene. The proteins encoded by this gene are p17 as the amino-terminal protein, p24 as the middle peptide, and p15 as the carboxyl-terminal end. A monoclonal antibody recognizing an antigenic determinant on a fragment of p15 has been developed and designated M35/2F8. This monoclonal has been instrumental in radiosequencing the carboxyl-terminal product of p15, p6, and in determining the cleavage site between this protein and the amino-terminal product, p7. By immunoaffinity chromatography it was also possible to purify p6 from HIV lysates and all p6 containing polyproteins from HIV-infected cells. These results gave more insight into the composition and processing of the HIV gag gene.
Keywords: Antibodies, Monoclonal/IMMUNOLOGY Antibodies, Viral/IMMUNOLOGY Chromatography, Affinity HIV/*ANALYSIS/IMMUNOLOGY Immunoelectrophoresis Peptide Fragments/IMMUNOLOGY Protein Processing, Post-Translational Retroviridae Proteins/BIOSYNTHESIS/IMMUNOLOGY/*ISOLATION & PURIF Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE

KWDantibodies,monoclonal/immunologyantibodies,viral/immunologychromatography,affinityhiv/KWDanalysis/immunologyimmunoelectrophoresispeptidefragments/immunologyproteinprocessing,post-translationalretroviridaeproteins/biosynthesis/immunology/KWDisolation&purifsupport,uKWDsKWDgov't,pKWDhKWDsKWDjournalarticle
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