CHROMATOGRAPHY
Online ISSN : 1348-3315
Print ISSN : 1342-8284
Original Papers
Enzyme Inhibitory Activity of Ovomucoid Extracted Using a Carboxypeptidase Y-Immobilized Membrane
Youji SHIMAZAKIKosuke TANAKAKeisuke SAKATA
Author information
JOURNALS FREE ACCESS

Volume 39 (2018) Issue 1 Pages 33-39

Details
Download PDF (1679K) Contact us
Abstract

Reversible inhibition of enzymes is caused by association and dissociation between enzymes and inhibitors. Therefore, reversible inhibitors can be trapped and extracted using enzyme-inhibitor interaction. The purpose of this study was to establish a method in which the reversible inhibitors retaining the original inhibitory activities are extracted from a single drop of biological sample using the enzyme-inhibitor interaction on the surface of a membrane. A membrane-immobilized carboxypeptidase Y (CPY) was produced after the biotinylated CPY was bound to the avidin separated by nondenaturing electrophoresis, transferred to a polyvinylidene fluoride and stained by Ponceau S. Ovomucoid, possessing reversible CPY inhibitory activity, was trapped and extracted from a single drop of egg white and isolated using the membrane-immobilized CPY. The isolated ovomucoid using this membrane-immobilized CPY possessed a feature that more than 85 % of the relative carboxylesterase activity was suppressed. The results indicate that ovomucoid retaining enzyme inhibitory activities can be isolated from a single drop of egg white sample using enzyme-immobilized membrane.

Information related to the author
© 2018 The Society for Chromatographic Sciences
Previous article Next article

Recently visited articles
feedback
Top