Adaptation of the plasma renin radioimmunoassay for use with HIV-1 protease. Academic Article

abstract

• We have demonstrated the use of a radioimmunoassay to quantitate the peptidolytic activity of human immunodeficiency virus, type 1 (HIV-1) protease using a tetradecapeptide substrate of porcine renin, Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser. HIV-1 protease catalyzes cleavage of this substrate at the same Leu-Leu bond as does porcine renin, resulting in the formation of authentic angiotensin-I. The angiotensin-I product is then detected by use of a commercially available renin plasma assay kit, which constitutes the basis of the RIA. The radioimmunoassay provides detection of the protease-catalyzed formation of angiotensin-I at picomolar concentrations in vitro. We demonstrate the use of this assay in determining IC50 values for two HIV-1 protease inhibitors present in cell culture media and in standard assay buffer. An example of the potential development of this assay for the quantitation of these inhibitors present in ex vivo plasma samples is also presented.

authors

• Meek, Thomas

published proceedings

• Anal Biochem

author list (cited authors)

• Hyland, L. J., & Meek, T. D.

citation count

• 5

complete list of authors

• Hyland, LJ||Meek, TD

publication date

• January 1991

publisher

• Elsevier  Publisher

published in

• Analytical Biochemistry  Journal

keywords

• Amino Acid Sequence
• Animals
• Hiv Protease
• Hiv Protease Inhibitors
• Humans
• In Vitro Techniques
• Molecular Sequence Data
• Peptides
• Protease Inhibitors
• Radioimmunoassay
• Renin
• Substrate Specificity
• Swine

Digital Object Identifier (DOI)

• 10.1016/0003-2697(91)90382-4

start page

• 225

end page

• 230

volume

• 197

issue

• 1

URL

• http://dx.doi.org/10.1016/0003-2697(91)90382-4