Document 0675
 DOCN  M9650675
 TI    Inhibition of dipeptidyl peptidase IV (DP IV) by anti-DP IV antibodies
       and non-substrate X-X-Pro- oligopeptides ascertained by capillary
       electrophoresis.
 DT    9605
 AU    Hoffmann T; Reinhold D; Kahne T; Faust J; Neubert K; Frank R; Ansorge S;
       Center of Internal Medicine, Otto-von-Guericke University; Magdeburg,
       Germany.
 SO    J Chromatogr A. 1995 Nov 17;716(1-2):355-62. Unique Identifier :
       AIDSLINE MED/96104282
 AB    Dipeptidyl peptidase IV (DP IV)-catalyzed hydrolysis of the
       NH2-X-Pro-containing N-terminal dodecapeptide of IL-2 was studied using
       free zone capillary electrophoresis as an alternative peptidase assay.
       In contrast to the conventional DP IV substrate
       glycyl-prolyl-p-nitroanilide (Gly-Pro-pNA), the hydrolysis of this
       peptide by DP IV was found to be significantly inhibited by anti-DP IV
       antibodies. Inhibition of DP IV was also observed with a number of
       non-substrate oligopeptides containing an N-terminal X-X-Pro- structure,
       including the HIV Tat protein. For Met-IL-2(1-6), we determined a
       competitive inhibition with an inhibition constant of ca. 100 microM.
 DE    Amino Acid Sequence  Antibodies/*IMMUNOLOGY/ISOLATION & PURIF  Antigens,
       CD26/*IMMUNOLOGY/METABOLISM  Electrophoresis, Capillary  Gene Products,
       tat/IMMUNOLOGY  Human  Hydrolysis  HIV Envelope Protein
       gp120/IMMUNOLOGY/ISOLATION & PURIF  Kinetics  Molecular Sequence Data
       Oligopeptides/METABOLISM/PHARMACOLOGY  Support, Non-U.S. Gov't  JOURNAL
       ARTICLE

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