Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168.
1991
Abstract
Two alkaline phosphatases were extracted from the membranes of Bacillus subtilis 168 stationary-phase cells and purified as homogeneous proteins by hydroxyapatite column chromatography. Alkaline phosphatases I and II differed in several properties such as subunit molecular weight, substrate specificity, thermostability, Km, pH stability, and peptide maps.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
9
References
9
Citations
NaN
KQI