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. 1988 Apr;86(4):1179–1184. doi: 10.1104/pp.86.4.1179

Identification and Purification of a Derepressible Alkaline Phosphatase from Anacystis nidulans R2 1

Maryse A Block 1,2,2, Arthur R Grossman 1,2
PMCID: PMC1054648  PMID: 16666051

Abstract

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 Mr 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 Mr 160,000 inhibit phosphatase activity by approximately 70%.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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