The effective use of immobilized anhydrotrypsin for the isolation of biologically active peptides containing L-arginine residues in C-termini
1976; Elsevier BV; Volume: 72; Issue: 4 Linguagem: Inglês
10.1016/s0006-291x(76)80175-1
ISSN1090-2104
AutoresHideyoshi Yokosawa, Shinichi Ishii,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoAnhydrotrypsin 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.
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