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M9490083.TXT
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1994-09-03
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Document 0083
DOCN M9490083
TI Characterization of a monoclonal antibody produced in an attempt to
mimic the active site of HIV aspartyl protease using haptens based on
inhibitor models.
DT 9411
AU Hanin V; Campagne JM; Dominice C; Mani JC; Dufour MN; Jouin P; Pau B;
Immunoanalyse et Innovation en Biologie Clinique, CNRS UMR 9921,;
Faculte de Pharmacie, Montpellier, France.
SO J Immunol Methods. 1994 Aug 1;173(2):139-47. Unique Identifier :
AIDSLINE MED/94321800
AB The high binding affinity and specificity of antibodies for a great
variety of ligands has been widely exploited in structure-activity
relationship studies of biomolecules and more recently in the
development of new catalysts for several chemical reactions. It is
assumed that antibodies generated against haptenic protease inhibitors
would recognize both these haptens and the substrate of the model
proteolytic reaction. We have produced antibodies against HIV PRp12
aspartyl protease substrate analogues, chemically modified at the
scissile bond, Phe-Pro. Identical chemical modifications have been
reported for related HIV protease inhibitors. We finally selected an
anti-hapten monoclonal antibody that specifically recognized the
substrate and those haptens with both the phenylalanyl side chain and
the prolyl pyrrolidine ring. This selectivity of recognition suggests
that such an antibody might mimic the catalytic site of the model
protease.
DE Amino Acid Sequence Animal Antibodies,
Monoclonal/BIOSYNTHESIS/*IMMUNOLOGY Antibody Specificity Binding,
Competitive Chromatography, Affinity Cross Reactions Enzyme-Linked
Immunosorbent Assay Haptens/CHEMISTRY/*IMMUNOLOGY Hybridomas
HIV/*ENZYMOLOGY/IMMUNOLOGY HIV Protease/CHEMISTRY/*IMMUNOLOGY HIV
Protease Inhibitors/CHEMISTRY/*IMMUNOLOGY Immune Sera/IMMUNOLOGY Mice
Mice, Inbred BALB C Molecular Sequence Data Peptide
Fragments/CHEMISTRY/IMMUNOLOGY Support, Non-U.S. Gov't JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).