Platt M W, Reizer J, Rottem S
Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
J Bacteriol. 1990 May;172(5):2808-11. doi: 10.1128/jb.172.5.2808-2811.1990.
Phosphorylation of a major 57-kilodalton protein substrate was observed in cell lysates of Spiroplasma melliferum BC3 incubated with [gamma-32P]ATP. Only serine phosphates have been isolated from the acid hydrolysate of the phosphorylated protein. The 57-kilodalton protein substrate was found, to a large extent, in the cytosolic fraction and, to a lesser extent, associated with cell membranes and was detected in the Triton X-100-insoluble fraction that contained fibrils.
在用[γ-32P]ATP孵育的蜂蜜螺旋体BC3细胞裂解物中观察到一种主要的57千道尔顿蛋白质底物的磷酸化。从磷酸化蛋白质的酸水解产物中仅分离出丝氨酸磷酸盐。发现57千道尔顿蛋白质底物在很大程度上存在于胞质部分,在较小程度上与细胞膜相关,并在含有原纤维的Triton X-100不溶性部分中检测到。