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Biomedical chromatography : BMC

Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone.


PMID 15236443

Abstract

The purpose of the present study was to determine the proteins that bind to acetophenones in the liver. Immobilized p-hydroxyacetophenone (p-HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that five polypeptides in the liver cytosolic fraction specifically bound to the p-HAP matrix. These polypeptides were digested with Lys-specific protease and used to generate peptide maps by reversed-phase high-performance liquid chromatography. Consequently, identification from a data base of protein sequences revealed that the five polypeptides were glycogen phosphorylase, cytosolic aldehyde dehydrogenase, adenosine kinase, class I alcohol dehydrogenase and glutathione S-transferase A2. In addition to p-HAP, acetylsalicylic acid also displayed a prominent ability to elute these five enzymes from the p-HAP affinity column loaded with the cytosolic fraction of the liver. Thus, p-HAP has affinities to the above liver enzymes and is a useful ligand for analysis of them.

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278564
4′-Hydroxyacetophenone, 99%
C8H8O2