产品
编 号：F466581
分子式：C17H25NO7
分子量：355.38
分子式：C17H25NO7
分子量：355.38
产品类型
规格
价格
是否有货
1mg
询价
询价
结构图
CAS No: 80879-63-6
产品详情
生物活性：
Emiglitate (BAY o 1248) is a potent, selective and competitive inhibitor of α-glucoside hydrolase.
体内研究：
In fasted rats, emiglitate inducec a significant, dose-dependent increase of hepatic glycogen concentrations. The increase in hepatic glycogen is due to lysosomal storage of glycogen only. Emiglitate in the amount of 5 mg/kg b.wt. does not induce significant changes either of glycogen concentrations or at the EM-level.
体外研究：
Emiglitate greatly suppresses the glucose-stimulated insulin release in parallel with an inhibitory effect on the activities of acid glucan-1,4-α-glucosidase and acid α-glucosidase. In contrast, the activities of acid phosphatase and N-acetyl-β-D-glucosaminidase tend to increase in the presence of the α-glucoside hydrolase inhibitor. The CO-induced amplification of the glucose-stimulated insulin release as well as of the increased activities of the acid α-glucoside hydrolases are abrogated by emiglitate and displayed the same levels as in the absence of CO. The CO-induced rise in the activities of acid phosphatase and acid N-acetyl-β-D-glucosaminidase is not appreciably affected by emiglitate.
Emiglitate (BAY o 1248) is a potent, selective and competitive inhibitor of α-glucoside hydrolase.
体内研究：
In fasted rats, emiglitate inducec a significant, dose-dependent increase of hepatic glycogen concentrations. The increase in hepatic glycogen is due to lysosomal storage of glycogen only. Emiglitate in the amount of 5 mg/kg b.wt. does not induce significant changes either of glycogen concentrations or at the EM-level.
体外研究：
Emiglitate greatly suppresses the glucose-stimulated insulin release in parallel with an inhibitory effect on the activities of acid glucan-1,4-α-glucosidase and acid α-glucosidase. In contrast, the activities of acid phosphatase and N-acetyl-β-D-glucosaminidase tend to increase in the presence of the α-glucoside hydrolase inhibitor. The CO-induced amplification of the glucose-stimulated insulin release as well as of the increased activities of the acid α-glucoside hydrolases are abrogated by emiglitate and displayed the same levels as in the absence of CO. The CO-induced rise in the activities of acid phosphatase and acid N-acetyl-β-D-glucosaminidase is not appreciably affected by emiglitate.
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