H. Yokosawa, S. Ishii
Oct 18, 1976
Citations
0
Influential Citations
16
Citations
Journal
Biochemical and biophysical research communications
Abstract
Summary Anhydrotrypsin immobilized on Sepharose has a specific affinity for the derivative of L-arginine whose carboxyl group is free. The chromatographic resolution of benzoyl-D- and -L-arginine is attainable on a column of this Sepharose derivative. Biologically-active arginine peptides, such as methionyl-lysyl-bradykinin, tuftsin and fibrinopeptide A, are able to be adsorbed tightly on this column and desorbed with 5 mM HCl; the behavior suggests the usefulness of anhydrotrypsin-Sepharose for the search and isolation of novel biologically-active peptides. The affinities for various ligands are also compared by frontal analysis.