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Original Articles

MECHANISTIC ASPECTS OF THE STEREOSPECIFIC INTERACTIONS OF IMMOBILIZED α1-ACID GLYCOPROTEIN

, , , &
Pages 813-825 | Received 22 Aug 2000, Accepted 08 Sep 2000, Published online: 06 Feb 2007
 

Abstract

The stereospecific interaction of a neutral probe molecule, acetonide, with immobilized α1-acid glycoprotein (AGP) was investigated. Enantioselectivity was found to be influenced by the choice of organic modifier, temperature, and pH. These parameters could be varied to the extent that a reversal of elution order could be induced. Our studies found that the role of hydrogen bonding in the chiral discrimination of acetonide was minimal. An inclusion mechanism is proposed with the investigated parameters affecting the access to the binding sites either through induced conformational changes or steric hindrance.

Acknowledgments

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