Skip to main content
Log in

Purification of bovine and porcine enterokinase by affinity chromatography with immobilized kidney bean enterokinase inhibitor

  • Published:
Journal of Biosciences Aims and scope Submit manuscript

Abstract

A specific enterokinase inhibitor isolated from kidney bean (Phaseolus vulgaris) was immobilized on Affigel-10. Solubilized preparation of bovine and porcine enterokinases were bound to this matrix at pH 7.5 and the complex was dissociated by elution with l0 mM HCl, resulting in the isolation of the enzymes in homogeneous form as judged by gel chromatography on Sephadex G-200, and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. However, human enterokinase could not be purified by this method in sufficient yield since it did not bind strongly to the insolubilized inhibitor.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

BAPNA:

α-N-Benzoyl DL-argininep-nitroanilide

Mr :

molecular weight

SDS:

sodiumdodecyl sulphate

PAGE:

Polyacrylamide gel electrophoresis

References

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jacob, R.T., Pattabiraman, T.N. Purification of bovine and porcine enterokinase by affinity chromatography with immobilized kidney bean enterokinase inhibitor. J Biosci 6, 289–295 (1984). https://doi.org/10.1007/BF02716743

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02716743

Keywords

Navigation