Chromophoric peptide substrates for the spectrophotometric assay of HIV-1 protease.
Biochem Biophys Res Commun
; 168(1): 274-80, 1990 Apr 16.
Article
en En
| MEDLINE
| ID: mdl-2183799
ABSTRACT
Purified HIV-1 protease hydrolyzes H-Ser-Gln-Asn-Leu-Phe(NO2)-Leu-Asp-Gly-NH2 (Peptide 1) and acetyl-Arg-Lys-Ile-Leu-Phe(NO2)-Leu-Asp-Gly-NH2 (Peptide 2) between the (p-nitro)phenylalanyl and leucyl residues. The cleavage of Peptides 1 and 2 resulted in a decrease in uv absorbance at 310 nm. The HIV-1 protease-catalyzed peptidolysis of Peptides 1 and 2 was characterized by a linear time course at substrate turnover of less than 20%. The solubilities of these substrates at pH 5.0 were sufficient to provide initial rate measurements over a concentration range of 0.05-0.5 mM. Steady-state kinetic data and inhibition constants using both spectrophotometric and high performance liquid chromatography (HPLC) analysis of the peptidolysis of these substrates resulted in comparable values.
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Banco de datos:
MEDLINE
Asunto principal:
Endopeptidasas
/
Productos del Gen pol
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1990
Tipo del documento:
Article