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Kinins—II pp 15-27 | Cite as

Specific Isolation of Biologically-Active Peptides by Means of Immobilized Anhydrotrypsin and Anhydrochymotrypsin

  • S. Ishii
  • H. Yokosawa
  • S. Shiba
  • K. Kasai
Part of the Advances in Experimental Medicine and Biology book series (AEMB)

Abstract

Anhydrotrypsin, a derivative of bovine trypsin, immobilized on Sepharose tightly adsorbs various peptides containing L-arginine at the carboxyl termini, such as bradykinin and tuftsin. These peptides correspond to the specific products of the action of trypsin-like enzymes. Native trypsin immobilized on Sepharose does not show such strong affinity. Fragment 2, a peptide with 41 amino acid residues, which has been released together with bradykinin from bovine high-molecular-weight kininogen by the action of plasma kallikrein, is also adsorbed on the immobilized anhydrotrypsin. When only the carboxyl-terminal arginine is removed with carboxy-peptidase B, however, the peptide loses its adsorptive ability. Immobilized anhydrochymotrypsin, on the other hand, exerts specific affinity for the peptides which correspond to the products of chymotrypsin. These results suggest that the anhydro-derivatives of serine-proteases in general may be of great use in the affinity chromatography of respective series of various naturally occurring peptides.

Keywords

Affinity Chromatography Carboxyl Terminus Cyanogen Bromide Affinity Adsorbent Frontal Analysis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1979

Authors and Affiliations

  • S. Ishii
    • 1
  • H. Yokosawa
    • 1
  • S. Shiba
    • 1
  • K. Kasai
    • 1
  1. 1.Department of Biochemistry, Faculty of Pharmaceutical SciencesHokkaido UniversitySapporo 060Japan

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