关于可的松衍生物对溶酶体酸性α-葡萄糖苷酶激活作用的进一步观察
Further observations on the activation of lysosomal acid alpha-glucosidase by cortisone derivatives.
作者信息
Bourne E J, Clarke K, Pridham J B, Rowe J J
出版信息
Biochem J. 1973 Mar;132(3):435-8. doi: 10.1042/bj1320435.
Abstract
- Cortisone acetate activates the acid alpha-glucosidase in rat liver slices and in isolated liver lysosomes. 2. The reaction is steroid specific and moreover does not occur with lysosomal acid phosphatase or beta-galactosidase. 3. After pretreatment of the lysosomes with cortisone, substrate (maltose) binding to the soluble lysosomal acid alpha-glucosidase is not affected, but the steroid does increase the V(max.) value. Membrane-bound enzyme is not activated by cortisone. 4. 4-[(14)C]Cortisone is preferentially bound to the lysosomal membrane and the possible involvement of this structure in the activation phenomenon is discussed.
摘要
- 醋酸可的松可激活大鼠肝切片及分离的肝溶酶体中的酸性α-葡萄糖苷酶。2. 该反应具有甾体特异性，且溶酶体酸性磷酸酶或β-半乳糖苷酶不会发生此反应。3. 用可的松预处理溶酶体后，底物（麦芽糖）与可溶性溶酶体酸性α-葡萄糖苷酶的结合不受影响，但该甾体确实会增加V(max.)值。膜结合酶不会被可的松激活。4. 4-[(14)C]可的松优先结合于溶酶体膜，并讨论了该结构在激活现象中的可能作用。
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