Binding of a tritiated pepstatin analog to human renin

Journal Article · Thu Jan 01 00:00:00 EST 1987 · J. Cardiovasc. Pharmacol.; (United States)

DOI:https://doi.org/10.1097/00005344-198706107-00019· OSTI ID:6924605

Cumin, F; Nisato, D; Gagnol, J P; Corvol, P

The interaction between human renin and a potent pepstatin analog, SR 42128, has been investigated using binding studies. Binding and enzymatic assays were performed at pH 5.7 and pH 7.4. We found one specific inhibitor binding site per molecule of renin at both pH's. The dissociation constant (KD) obtained at equilibrium was 14-fold lower at pH 5.7 than at pH 7.4, showing a pH effect on binding of (/sup 3/H)SR 42128. A similar decrease was measured in enzymatic studies. In nonequilibrium conditions, we demonstrated that only association kinetic constants have been affected by pH variations. Radioligands provided interesting tools to investigate enzyme-inhibitor relationships.

• Research Organization: INSERM U36, Paris (France)
• OSTI ID: 6924605
• Journal Information: J. Cardiovasc. Pharmacol.; (United States), Journal Name: J. Cardiovasc. Pharmacol.; (United States)
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ENZYME INHIBITORS
BIOCHEMICAL REACTION KINETICS
RECEPTORS
RENIN
LIGANDS
PH VALUE
RADIOENZYMATIC ASSAY
TRACER TECHNIQUES
TRITIUM COMPOUNDS
ENZYMES
HYDROLASES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MEMBRANE PROTEINS
NONSPECIFIC PEPTIDASES
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PROTEINS
REACTION KINETICS
550201* - Biochemistry- Tracer Techniques