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- TAKAGI Shiro
- 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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- URAYAMA Tadanori
- Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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- SUZAWA Itsuko
- Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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- MATSUDA Kazuo
- Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University Present address: Iwaki-Meisei University
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- ICHISHIMA Eiji
- Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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Rabbit muscle phosphorylase b was modified with a substrate analog, the 2', 3'-dialdehyde derivative of α-cyclodextrin (dial-α-CD). Although the inhibition of phosphorylase b by α-, β-, and γ-cyclodextrins gave rather high Ki values (10-25 ITIM), the dial-CD gave much smaller Ki values of 1.2-3.5mM. Moreover, the latter inhibition was time-dependent and accelerated by higher pHs and higher concentrations of dial-CD. Incorporation of the dial-CD into the enzyme was proportional to the loss of enzyme activity and became stationary at about 1 mol of dial-CD bound to a mol of enzyme subunit. Modification was greatly suppressed by the presence of substrate glycogen. Glucose 1-phosphate was not effective. The dial-CD-modified phosphorylase b was purified by Sephadex G-75 and Con A-Sepharose column chromatography. The modified enzyme gave a single band of activity having a Kapp of 6.3% glycogen on affinity gel electrophoresis, which showed that the modified enzyme had a very low affinity for glycogen. Comparison of Km values of the native and modified phosphorylase b showed that the Km values for the glucan substrates increased 8 to 11-fold in the modified enzyme. These results suggested that the glycogen storage site of muscle phosphorylase b might be modified with dial-CD and the modified enzyme significantly decreased in the affinity for the substrate glycogen.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 52 (11), 2709-2716, 1988
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206464538112
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- NII論文ID
- 110006323529
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- NII書誌ID
- AA00515312
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- COI
- 1:CAS:528:DyaL1MXntFKrtg%3D%3D
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- ISSN
- 18811280
- 00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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- 使用不可