Purification of Glycogen Debranching Enzyme from Porcine Brain : Evidence for Glycogen Catabolism in the Brain
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概要
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Amylo-1,6-glucosidase from porcine brain was purified to homogeneity by ammonium sulfate fractionation, followed by sequential steps of liquid chromatography on DEAE-Sephacel, Sephacryl S-300, and Super Q. The purified enzyme had both maltooligosaccharide transferase and amylo-1,6-glucosidase activities within a single polypeptide chain, and the combination of these two activities removed the branches of phosphorylase limit dextrin. Based on these results, the purified enzyme was identified as a glycogen debranching enzyme (GDE). The molecular weight of the brain GDE was 170,000 by gel-filtration and 165,000 by reducing SDS–PAGE. The pH profile of maltooligosaccharide transferase activity coincided with that of the amylo-1,6-glucosidase activity (pH optimum at 6.0). The existence of GDE as well as glycogen phosphorylase in the brain explains brain glycogenolysis fully and supports the hypothesis that glycogen is a significant source of energy in this organ.
- 社団法人 日本農芸化学会の論文
- 2006-04-23
著者
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Omichi Kaoru
Department Of Chemistry Graduate School Of Science Osaka Prefecture University
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Omichi Kaoru
Department Of Applied Chemistry Waseda University
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Makino Yasushi
Department Of Chemistry Graduate School Of Science Osaka Prefecture University
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