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J. Biochem, 1988, Vol. 103, No. 2 297-301
© 1988 Japanese Biochemical Society

research-article

Immobilized Anhydrochymotrypsin as a Biospecific Affinity Adsorbent for the Peptides Produced by Chymotryptic Hydrolysis1

Takashi Kumazaki, Faculty of Pharmaceutical Sciences*, Asamichi Fujitani, Faculty of Pharmaceutical Sciences*, Kumiko Terasawa, Faculty of Pharmaceutical Sciences*, Kiyohito Shimura, Faculty of Pharmaceutical Sciences**, Ken-ichi Kasai, Faculty of Pharmaceutical Sciences** and Shin-ichi Ishii, Faculty of Pharmaceutical Sciences*

*Department of Biochemistry,Hokkaido University Kita-ku, Sapporo, Hokkaido 060
**Department of Biochemistry,Teikyo University Sagamiko, Kanagawa 199-01

Anhydrochymotrypsin immobilized on Sepharose specifically adsorbed various peptides containing L-tryptophan, L-tyrosine, or L-phenylalanine residues at their carboxy-termini. These peptides correspond to the specific products of chymotryptic cleavage of polypeptides. A mixture of the chymotryptic peptides once adsorbed on the column could be effectively separated by eluting them with a pH gradient. This adsorbent, on the other hand, showed no substantial affinity toward the substrate-type peptides that contain the aromatic amino acid(s) within the peptide chain, or toward the C-terminal leucine peptides. By taking advantage of this unique property of anhydrochymotrypsin-Sepharose in combination with reversed-phase high-performance liquid chromatography, we have succeeded in separating the C-terminal peptides from chymotryptic digests of reduced and S-carboxymethylated bovine insulin and from tryptic digests from reduced and S-carboxymethylated Streptomyces subtilisin inhibitor.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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