Inhibition of the aspartic proteinase from HIV-2.
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.
Richards
A D
AD
Dept of Biochemistry, University of Wales College of Cardiff.
Broadhurst
A V
AV
Ritchie
A J
AJ
Dunn
B M
BM
Kay
J
J
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
D011480:Protease Inhibitors; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases