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

Journal of Biochemistry
H YokosawaS Ishii

Abstract

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, which was easily prepared by coupling a tryptic digest of salmine to cyanogen bromide-activated Sepharose 4B, was required. A high degree of homogeneity was demonstrated for the purified enzyme by disc electrophoresis, SDS-polyacrylamide gel electrophoresis and gel filtration, as well as by active-site titration. The behavior of a carboxypeptides B [EC 3.4.12.3]-like enzyme present in Pronase is also discussed.

References

Jun 1, 1984·Applied Biochemistry and Biotechnology·B M Dunn
Sep 1, 1996·Biomedical Chromatography : BMC·X Wu, G Liu
Jan 15, 1988·European Journal of Biochemistry·A OkitaniM Fujimaki
Oct 10, 2002·Journal of Peptide Science : an Official Publication of the European Peptide Society·Haruo SekizakiKazutaka Tanizawa

Related Concepts

Salmine
Protamine Sulfate (USP)
Polyacrylamide Gels
Enzymes, antithrombotic
Cathepsin G
Chromatography
Plasma Protein Binding Capacity
Trypsin
Bromides Measurement
Gel Chromatography

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