Chromophoric peptide substrates for the spectrophotometric assay of HIV-1 protease. Academic Article

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.

authors

• Meek, Thomas

published proceedings

• Biochem Biophys Res Commun

altmetric score

• 6

author list (cited authors)

• Tomaszek, T. A., Magaard, V. W., Bryan, H. G., Moore, M. L., & Meek, T. D.

citation count

• 38

complete list of authors

• Tomaszek, TA||Magaard, VW||Bryan, HG||Moore, ML||Meek, TD

publication date

• January 1990

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Amino Acid Sequence
• Chromatography, High Pressure Liquid
• Endopeptidases
• Gene Products, Pol
• HIV-1
• Hiv Protease
• Hydrogen-Ion Concentration
• Kinetics
• Molecular Sequence Data
• Oligopeptides
• Recombinant Proteins
• Spectrophotometry

Digital Object Identifier (DOI)

• 10.1016/0006-291x(90)91704-v

start page

• 274

end page

• 280

volume

• 168

issue

• 1

URL

• http://dx.doi.org/10.1016/0006-291x(90)91704-v