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.
Preclinical Research, Sandoz Pharma Ltd, Basle, Switzerland.
J P
JP
Evenou
B
B
Weidmann
A
A
Hagenbach
R
R
Metternich
E
E
Pfenninger
H
H
Wagner
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