通过扫描隧道显微镜和原子力显微镜直接观察磷酸化酶-磷酸化酶激酶复合物

Edstrom R D, Meinke M H, Yang X R, Yang R, Elings V, Evans D F

Department of Biochemistry, Medical School, University of Minnesota, Minneapolis 55455.

Biophys J. 1990 Dec;58(6):1437-48. doi: 10.1016/S0006-3495(90)82489-9.

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.

在骨骼肌中，磷酸化酶b的激活由磷酸化酶激酶催化。这两种酶在体内作为多酶复合物的一部分存在。已通过原子力显微镜对这两种酶进行成像，并将结果与先前通过扫描隧道显微镜获得的结果进行比较。扫描隧道显微镜和原子力显微镜已用于观察激活酶磷酸化酶激酶与其底物磷酸化酶b之间的复合物。当磷酸化酶激酶与磷酸化酶b结合时，观察到其大小和形状发生了变化。