Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy.
Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy.
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DOI：
10.1016/s0006-3495(90)82489-9
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发表时间：
1990-12
影响因子：
3.4
通讯作者：
Ronald D. Edstrom;M. Meinke;Xiuru Yang;Rui Yang;Virgil B. Elings;D. F. Evans
中科院分区：
文献类型：
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作者：
Ronald D. Edstrom;M. Meinke;Xiuru Yang;Rui Yang;Virgil B. Elings;D. F. Evans
在骨骼肌中，磷酸化酶b的激活是由磷酸化酶激酶催化的。这两种酶在体内都作为多酶复合体的一部分存在。这两种酶已经用原子力显微镜进行了成像，并与以前通过扫描隧道显微镜发现的结果进行了比较。用扫描隧道显微镜和原子力显微镜观察了激活酶磷酸化酶与其底物磷酸化酶b之间的络合物，观察到磷酸化酶与磷酸化酶b结合后，磷酸化酶的大小和形状发生了变化。
In skeletal muscle the activation of phosphorylase b is catalyzed by phosphorylase kinase. Both enzymes occur in vivo as part of a multienzyme complex. The two enzymes have been imaged by atomic force microscopy and the results compared to those previously found by scanning tunneling microscopy. Scanning tunneling microscopy and atomic force microscopy have been used to view complexes between the activating enzyme phosphorylase kinase and its substrate phosphorylase b. Changes in the size and shape of phosphorylase kinase were observed when it bound phosphorylase b.