Carnegie Institution of Washington, Stanford, California 94305.
Plant Physiol. 1988 Apr;86(4):1179-84. doi: 10.1104/pp.86.4.1179.
We have examined the increase in alkaline phosphatase activity in the cyanobacterium Anacystis nidulans R2 upon phosphate deprivation. Much of the activity is released into the medium when A. nidulans is osmotically shocked, indicating that the enzyme is located either in the periplasmic space or is loosely bound to the cell wall. The polypeptide associated with phosphatase activity has been identified as a single species of M(r) 160,000. Several lines of evidence demonstrate that this polypeptide is responsible for alkaline phosphatase activity: (a) It is absent when cells are grown in the presence of phosphate and specifically accumulates during phosphate deprivation. (b) It is the major periplasmic polypeptide extracted by osmotic shock. (c) It represents over 90% of the protein in a fraction of periplasmic polypeptides enriched for phosphatase activity. (d) Antibodies raised against the purified species of M(r) 160,000 inhibit phosphatase activity by approximately 70%.
我们研究了缺磷时蓝藻鱼腥藻 R2 碱性磷酸酶活性的增加。当鱼腥藻受到渗透冲击时，大部分活性被释放到培养基中，表明该酶位于周质空间或与细胞壁松散结合。与磷酸酶活性相关的多肽已被鉴定为一种分子量为 160,000 的单一物种。有几条证据表明，这种多肽负责碱性磷酸酶活性：（a）当细胞在磷酸盐存在下生长时，它不存在，并且在磷酸盐缺乏时特异性积累。（b）它是渗透压冲击提取的主要周质多肽。（c）它代表富含磷酸酶活性的周质多肽级分中蛋白质的 90%以上。（d）针对纯化的 Mr160,000 物种产生的抗体通过大约 70%抑制磷酸酶活性。
Zotero 插件
