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. 1970 Nov;104(2):748–753. doi: 10.1128/jb.104.2.748-753.1970

Release of Alkaline Phosphatase from Cells of Pseudomonas aeruginosa by Manipulation of Cation Concentration and of pH1

K-J Cheng a,2, J M Ingram a, J W Costerton a,3
PMCID: PMC285053  PMID: 4992367

Abstract

Pseudomonas aeruginosa ATCC 9027 contains an inducible alkaline phosphatase. The enzyme is readily removed from 14-hr cells by washes in 0.2 m MgCl2, pH 8.4. Similar washes in tris(hydroxymethyl)aminomethane buffer, 20% sucrose, monovalent ions, or water partially release enzyme from the cells. The release of alkaline phosphatase is correlated with an increased release of protein and retention of internal enzymes. The effect of 0.2 m MgCl2 washing upon the cells is minimal since both viability and growth rates remain unchanged as compared to water washing. Although cells are plasmolyzed in both 0.2 m MgCl2 and 20% sucrose, it is evident that plasmolysis alone is unable to account for total enzyme release and that a divalent metal, i.e. Mg2+, augments the release pattern. Growing cells in the presence of increasing concentrations of MgCl2 or at increased pH values results in an almost total secretion of the enzyme to the culture filtrate. The findings suggest that P. aeruginosa alkaline phosphatase is linked to the exocytoplasmic region through divalent metal ion, presumably Mg2+, bridges.

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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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