Purification of bovine and porcine enterokinase by affinity chromatography with immobilized kidney bean enterokinase inhibitor.
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Date
1984-09
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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 7ยท5 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.
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Keywords
Affinity chromatography, enterokinase isolation, bovine and porcine, kidney bean enterokinase inhibitor
Citation
Jacob Raju Thomas, Pattabiraman T N. Purification of bovine and porcine enterokinase by affinity chromatography with immobilized kidney bean enterokinase inhibitor. Journal of Biosciences. 1984 Sept; 6(3): 289-295.