Immobilized anhydrotrypsin as a specific affinity adsorbent for tryptic peptides.

@article{Ishii1983ImmobilizedAA,
  title={Immobilized anhydrotrypsin as a specific affinity adsorbent for tryptic peptides.},
  author={S. Ishii and H. Yokosawa and T. Kumazaki and I. Nakamura},
  journal={Methods in enzymology},
  year={1983},
  volume={91},
  pages={
          378-83
        }
}

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References

SHOWING 1-10 OF 17 REFERENCES
The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
TLDR
The structure of the complex between anhydro-trypsin and pancreatic trypsin inhibitor has been determined by difference Fourier techniques using phases obtained from the native complex by constrained crystallographic refinement at 1.9 å resolution. Expand
Immobilized anhydrotrypsin as a biospecific affinity adsorbent for the peptides produced by trypsin-like proteases.
TLDR
The peptide fragments in the tryptic digests of reduced and S-carboxymethylated erabutoxin a were also fractionated effectively by chromatography on this affinity adsorbent, and fragments containing l -lysine at the carboxyl termini showed weaker affinity for the Adsorbent than those containing l-arginine atThe termini. Expand
Mechanism of association of a specific aldehyde inhibitor, leupeptin, with bovine trypsin.
TLDR
The pH dependencies of the dissociation constant and other parameters show that deprotonation of the charge-relay sustem in the active site is important for the formation and stabilization of complex II, suggesting that complex II consists of a covalent hemiacetal adduct formed between the serine hydroxyl group in the enzyme active site and the aldehyde group inThe inhibitor. Expand
Anhydrotrypsin: new features in ligand interactions revealed by affinity chromatography and thionine replacement.
TLDR
Comparative studies of the ligand interaction specificities with anhydrotrypsin and trypsin confirmed the stronger interaction of the former protein with product-type ligands such as Bz-Arg-OH, while the higher affinity of anhyd rotarypsin was found to be limited to product- type ligands of L-configuration. Expand
Correction of partial amino acid sequence of erabutoxins.
The amino acid sequences of erabutoxins a and b were re-examined. The previously reported sequence of Ser-Glu at positions 21 and 22 of erabutoxins was corrected to Glu-Ser.
Affinity chromatography of trypsin and related enzymes. III. Purification of Streptomyces griseus trypsin using an affinity adsorbent containing a tryptic digest of protamine as a ligand.
A new, simple method has been developed for the purification of Streptomyces griseus trypsin [EC 3.4.21.4] from Pronase. Only a single operation of affinity chromatography on an agarose derivative,Expand
The effective use of immobilized anhydrotrypsin for the isolation of biologically active peptides containing L-arginine residues in C-termini.
  • H. Yokosawa, S. Ishii
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1976
TLDR
Anhydrotrypsin immobilized on Sepharose has a specific affinity for the derivative of L-arginine whose carboxyl group is free, suggesting the usefulness of anhydrotarypsin-Sepharose for the search and isolation of novel biologically-active peptides. Expand
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