Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168.
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.
Sugahara
T
T
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Konno
Y
Y
Ohta
H
H
Ito
K
K
Kaneko
J
J
Kamio
Y
Y
Izaki
K
K
D000469:Alkaline Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002845:Chromatography; D017886:Durapatite; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D006882:Hydroxyapatites; D007527:Isoenzymes; D010446:Peptide Fragments; D017886:Durapatite; D000469:Alkaline Phosphatase; D014357:Trypsin