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- W2315155203 abstract "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 mm), the dial-CD gave much smaller Ki values of 1.2~3.5 mm. 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..." @default.
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- W2315155203 date "1988-11-01" @default.
- W2315155203 modified "2023-09-27" @default.
- W2315155203 title "Affinity Labeling of Muscle Phosphorylasebwith α-Cyclodextrin-Dialdehyde" @default.
- W2315155203 doi "https://doi.org/10.1080/00021369.1988.10869125" @default.
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