Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168

T Sugahara; Y Konno; H Ohta; K Ito; J Kaneko; Y Kamio; K Izaki

doi:10.1128/jb.173.5.1824-1826.1991

Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168

J Bacteriol. 1991 Mar;173(5):1824-6. doi: 10.1128/jb.173.5.1824-1826.1991.

Authors

T Sugahara¹, Y Konno, H Ohta, K Ito, J Kaneko, Y Kamio, K Izaki

Affiliation

¹ Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.

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.

MeSH terms

Alkaline Phosphatase / isolation & purification*
Alkaline Phosphatase / metabolism
Bacillus subtilis / enzymology*
Cell Membrane / enzymology
Chromatography
Durapatite
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Hydroxyapatites
Isoenzymes / isolation & purification*
Isoenzymes / metabolism
Kinetics
Molecular Weight
Peptide Fragments / isolation & purification
Trypsin

Substances

Hydroxyapatites
Isoenzymes
Peptide Fragments
Durapatite
Alkaline Phosphatase
Trypsin