A novel method for selective isolation of C-terminal peptides from tryptic digests of proteins by immobilized anhydrotrypsin: Application to structural analyses of the tail sheath and tube proteins from bacteriophage T4-Reference-Cited by-同舟云学术

A novel method for selective isolation of C-terminal peptides from tryptic digests of proteins by immobilized anhydrotrypsin: Application to structural analyses of the tail sheath and tube proteins from bacteriophage T4

Published:1986-01 Issue:1 Volume:1 Page:100-107
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Kumazaki Takashi,Nakako Tatsushi,Arisaka Fumio,Ishii Shin-Ichi

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference23 articles.

1. Anhydrotrypsin: New Features in Ligand Interactions Revealed by Affinity Chromatography and Thionine Replacement1

2. The effective use of immobilized anhydrotrypsin for the isolation of biologically active peptides containing L-arginine residues in C-termini

3. Immobilized anhydrotrypsin as a biospecific affinity adsorbent for the peptides produced by trypsin-like proteases

4. Immobilized anhydrotrypsin as a specific affinity adsorbent for tryptic peptides. In: Enzyme Structure Part I. Methods in Enzymology Vol. 91. London: Academic Press. 1983:378-383

5. Affinity Chromatography of Trypsin and Related Enzymes: III. Purification of Streptomyces griseusTrypsin Using an Affinity Adsorbent Containing a Tryptic Digest of Protamine as a Ligand1

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