Phosphate modification of fructose-1,6-bisphosphate aldolase in Escherichia coli.
Phosphate modification of fructose-1,6-bisphosphate aldolase in Escherichia coli.
复制标题
大肠杆菌中果糖-1,6-二磷酸醛缩酶的磷酸修饰。
DOI：
10.1016/s0006-291x(88)80469-8
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发表时间：
1988
影响因子：
3.1
通讯作者：
Fraenkel,DG
中科院分区：
文献类型：
--
作者：
Babul,J;Fraenkel,DG
WhenE。在32pi的作用下培养了携带果糖-1,6-醛缩酶或磷酸甘油酸激酶的多拷贝质粒，SDS-PAGE后在同源高水平多肽的位置有标记。在醛缩酶测试中，该标记对丙酮、RNase和热TCA处理具有抗性，并通过纯化的醛缩酶进行免疫沉淀观察。在氯霉素存在的情况下也发生了标签合并。免疫沉淀也显示野生型菌株有明显的醛缩酶标记。
WhenE.colicarrying multicopy plasmids for fructose-1,6-P2aldolase or phosphoglycerate kinase was grown in the presence of32Pi, there was label at the position of cognate high level polypeptide after SDS-PAGE. As tested for aldolase, the label was resistant to acetone, RNase, and hot TCA treatments, and was also observed by immunoprecipitation, which was competed for by purified aldolase. Incorporation of label also occurred in the presence of chloramphenicol. Immunoprecipitation revealed apparent aldolase labeling in the wild type strain as well.