title: Inhibition of the aspartic proteinase from HIV-2.
abstract: Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.
authors.affiliation: Dept of Biochemistry, University of Wales College of Cardiff.
authors.forename: A D
authors.initials: AD
authors.lastname: Richards
authors.forename: A V
authors.initials: AV
authors.lastname: Broadhurst
authors.forename: A J
authors.initials: AJ
authors.lastname: Ritchie
authors.forename: B M
authors.initials: BM
authors.lastname: Dunn
authors.forename: J
authors.initials: J
authors.lastname: Kay
mesh_terms: D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases; D015498:HIV-2 / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
chemical_list: D011480:Protease Inhibitors; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases