Structural studies of staphylococcal protease. III. Binding of anions to the spin-labeled enzyme
-
Published:1978-01-01
Issue:1
Volume:56
Page:7-12
-
ISSN:0008-4018
-
Container-title:Canadian Journal of Biochemistry
-
language:en
-
Short-container-title:Can. J. Biochem.
Author:
Dugas Hermann,Gaudet Fernand,Leduc Paul
Abstract
The staphylococcal protease was coupled at the active-site serine residue with a spin-labeled analog of diisopropyl fluorophosphonate and the interaction of competitive inhibitors such as chloride and acetate anions, as well as N-carbobenzoxy-L-glutamic acid (Z-L-Glu), was investigated by electron paramagnetic resonance spectroscopy. It was observed that the addition of chloride ions to the spin-labeled enzyme increased the freedom of motion of the spin label while the presence of acetate ions and Z-L-Glu resulted in an increase in the immobilization of the spin label. These results suggest that these ions bind to the active site region in different ways.
Publisher
Canadian Science Publishing