Binding of a Bolton-Hunter substituted homostatine analog to affinity-immobilized human renin.
The binding of a Bolton-Hunter reagent substituted homostatine analog, SDZ 213-776, to human renin was investigated at pH 6.5 and 7.4. At both pH values, SDZ 213-776 bound to human renin in a reversible and saturable manner. The binding characteristics conformed to a one-site binding model. The dissociation constant Kd, obtained at equilibrium, was four-fold lower at pH 6.5 that at pH 7.4 (0.94 nM vs 3.7 nM). Under non-equilibrium conditions, only the association kinetic constant k+1 was affected by pH. The results of the binding assay at pH 6.5 correlated well with those obtained in enzymatic assay at the same pH.
Evenou
J P
JP
Preclinical Research, Sandoz Pharma Ltd, Basle, Switzerland.
Weidmann
B
B
Hagenbach
A
A
Metternich
R
R
Pfenninger
E
E
Wagner
H
H
D000911:Antibodies, Monoclonal; D001667:Binding, Competitive; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009842:Oligopeptides / Q000378:metabolism*; D012083:Renin / Q000378:metabolism; D013388:Succinimides; D000092502:Renin Inhibitors
D000911:Antibodies, Monoclonal; D004800:Enzymes, Immobilized; D009842:Oligopeptides; D012083:Renin; D013388:Succinimides; D000092502:Renin Inhibitors; C065366:SDZ 213-776; C022581:Bolton-Hunter reagent