1. An alkaline phosphatase was partially purified from extracts of Halobacterium cutirubrum. 2. The enzyme has a mol.wt. of 15 500 and is therefore less than one-quarter of the size of other known bacterial alkaline phosphatases. 3. It is stimulated up to ten-fold by Mn2+, but not by Ca2+ or Mg2+. 4. The activities with and without Mn2+ cannot be separated by gel filtration and have similar restricted substrate specificities. 5. The only substrates for the enzyme that have so far been found are p-nitrophenyl phosphate, 5'-dATP, 5'-dTMP and 5'-dTTP.
Research Article|July 01 1976
Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase
Biochem J (1976) 157 (1): 161-167.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
P S Fitt, P I Peterkin; Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase. Biochem J 1 July 1976; 157 (1): 161–167. doi: https://doi.org/10.1042/bj1570161
Download citation file: