Yeast Glycogen Phosphorylase: Characterization of the Dimeric Form and Its Activation
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概要
- 論文の詳細を見る
The purification of yeast glycogen phosphorylase [EC 2.4.1.1] was improved by ethanol precipitation and affinity chromatography on a glycogen-Sepharose column. The purified enzyme gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and had a subunit molecular mass of 100 kDa. Gel electrophoresis also showed that the major activity of native phosphorylase was ascribed to a dimer of 203 kDa, which was agreed with the value obtained by gel filtration on Sephadex G-200. The yeast phosphorylase showed a high affinity for AMP-Sepharose, whereas the enzyme was specifically inhibited by AMP. This inhibition was competitive with respect to the substrate glucose 1-phosphate and gave a Ki value of 9.3 mM. Activation of the crude extract by phosphorylation with an endogenous phosphorylase kinase indicated that the yeast phosphorylase occurred in a mixture of phosphorylated and non-phosphorylated forms.
- 社団法人 日本農芸化学会の論文
著者
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Tanabe Satoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Kobayashi Mikihiko
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Matsuda Kazuo
Department Of Agricultural Biochemistry Faculty Of Agriculture Tohoku University
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