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 plasm 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-proteseas in general may be of great use in the affinity chromatography of respective series of various naturally occurring peptides.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Ishii S,Yokosawa H,Shiba S,Kasai Kdoi
10.1007/978-1-4757-0926-1_3subject
Has Abstractpub_date
1979-01-01 00:00:00pages
15-27eissn
0065-2598issn
2214-8019journal_volume
120Apub_type
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