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).