Simple and unique purification by size-exclusion chromatography for an oligomeric enzyme,rat liver cytosolic acetyl-coenzyme A hydrolase |
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Authors: | Suematsu Naoya Okamoto Kazuki Isohashi Fumihide |
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Institution: | Department of Biochemistry, St. Marianna University School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki, 216-8511, Kanagawa, Japan. n2sue@marianna-u.ac.jp |
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Abstract: | An overview of the purification of an oligomeric enzyme, an extramitochondrial acetyl-coenzyme A hydrolase from rat liver, is presented. The enzyme has been purified to homogeneity using two successive size-exclusion chromatography runs, first for the monomeric and second for the oligomeric form of the enzyme. The sequential gel-filtration steps efficiently removed the contaminants of any molecular size, first of different size from that of the monomeric form of the enzyme (K(av)=0.47 on Superdex 200) and second of different size from that of the oligomeric form (K(av)=0.33), allowing us to purify the enzyme in high purity. This strategy provides an excellent model for purifying many other oligomeric proteins including key enzymes or allosteric enzymes regulating metabolism. |
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