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Inhibition of the aspartic proteinase from HIV‐2
Author(s) -
Richards Anthony D.,
Broadhurst Anne V.,
Ritchie Alison J.,
Dunn Ben M.,
Kay John
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80961-5
Subject(s) - pepstatin , proteinase 3 , chemistry , proteinase inhibitor , enzyme , substrate (aquarium) , human immunodeficiency virus (hiv) , biochemistry , protease , stereochemistry , virology , biology , antibody , immunology , ecology , autoantibody
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.