Affinity chromatography on immobilized anhydrotrypsin: general utility for selective isolation of C-terminal peptides from protease digests of proteins.

@article{Kumazaki1987AffinityCO,
  title={Affinity chromatography on immobilized anhydrotrypsin: general utility for selective isolation of C-terminal peptides from protease digests of proteins.},
  author={T. Kumazaki and K. Terasawa and S. Ishii},
  journal={Journal of biochemistry},
  year={1987},
  volume={102 6},
  pages={
          1539-46
        }
}
Recently we have succeeded in the efficient isolation of the C-terminal peptides from tryptic digests of the tail sheath protein (with C-terminal Gly) and the tube protein (with C-terminal Glu) of bacteriophage T4, by taking advantage of a unique property of immobilized anhydrotrypsin, that is, a strong specific affinity for peptides containing Arg or Lys residues at their C-termini. In this study, the utility of affinity chromatography on immobilized anhydrotrypsin was further demonstrated in… Expand
Selective isolation of C-terminal peptides from proteolytic mixtures of proteins by affinity chromatography on immobilized anhydrotrypsin and anhydrochymotrypsin
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Immobilized Anhydrotrypsin as a Specific Affinity Adsorbent for Polypeptides Containing Arginyl, Lysyl, or S-Aminoethylcysteinyl Residues at the C-termini
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A characteristic property of anhydrotrypsin, i.e., its ability to strongly bind C‐terminal arginine, proved to be useful as a tool for specific enrichment of a recombinant protein. An arginine tailExpand
Application of an anhydrotrypsin-immobilized precolumn for selectvie separation of peptides having arginine or lysine at theinr C-termini by column-switching high-performance liquid
A column-switching high-performance liquid chromatographic (CS-HPLC) system which consisted of an anhydrotrypsin (AHT)-immobilized diol—silica precolumn and a reversed-phase analytical column wasExpand
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  • Journal of chromatography
  • 1992
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Every protein expresses its function through its capability of specific molecular recognition, which depends on its three-dimensional structure. In order to understand the fundamental relationExpand
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SummaryAnhydrotrypsin (AHT), a catalytically inert derivative of trypsin in which the active site serine residue was converted to dehydroalanine residue by chemical modification, was immobilized ontoExpand
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SummaryAnhydrochymotrypsin (AHC), a catalytically inert derivative of chymotrypsin in which the serine-residue active site has been converted chemically to a dehydroalanine residue, was immobilizedExpand
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TLDR
Immobilized anhydroelastase was effectively isolated by a single operation of affinity chromatography from a complex mixture produced by phenylmethylsulfonylation and alkaline treatment of porcine pancreatic elastase and found to be useful in the purification and search for naturally occurring proteinase inhibitors. Expand
Improvement in Selectivity of Anhydrotrypsin-Immobilized Diol Silica Column by the Use of Eluent Containing Calcium Ion
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