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Comparative Study
. 1978 Oct 12;526(2):457-67.
doi: 10.1016/0005-2744(78)90137-7.

Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization

S D Schaffel, F M Hulett
Comparative Study

Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization

S D Schaffel et al. Biochim Biophys Acta. .

Abstract

The membrane-associated alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from Bacillus licheniformis MC14, a facultative thermophile, was purified to homogeneity in buffer containing 0.2 M Mg2+. The alkaline phosphatase purified in this manner is insoluble upon removal of the magnesium by dialysis. This insoluble alkaline phosphatase has been characterized and compared to the previously purified heat-solubilized enzyme (Hulett-Cowling, F.M. and Campbell, L.L. (1971) Biochemistry 10, 1364--1371).

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