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. 1977 Mar;129(3):1607–1612. doi: 10.1128/jb.129.3.1607-1612.1977

Biochemical and physiological properties of alkaline phosphatases in five isolates of marine bacteria.

H M Hassan, D Pratt
PMCID: PMC235141  PMID: 845125

Abstract

The alkaline phosphatase activities of five unique isolates of marine bacteria were found to be associated with the periplasmic space; however, the enzymes from these isolates differed with respect to their repressibility, the apparent number of isoenzymes, the necessity for Mg2 for activity, and the conditions required for their release. With three of the isolates, the enzyme was released when cells that had been washed in 0.5 M NaCl were suspended in sucrose; however, with the other two isolates, one required the additional presence of tris(hydroxymethyl)aminomethane and the other required the presence of lysozyme and ethylenediaminetetraacetic acid. In two isolates the activity was constitutive, in two it was partially repressed, and in one it was completely repressed by inorganic phosphate. The repression of activity was associated with corresponding changes of activity bands as seen by acrylamide gel electrophoresis.

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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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