Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity surpassed that of alkaline phosphatase from Escherichia coli. Phosphatase was also found in the culture liquid of P. mirabilis. The composition of proteins displaying enzyme activity was assayed by polyacrylamide gel electrophoresis. Enzyme synthesis was studied at various stages of bacterial growth. Biosynthesis of phosphatase in P. mirabilis (similarly to that in other bacteria) was shown to be induced under conditions of inorganic phosphate deficiency in the medium
The phosphate regulation and subcellular location of the hydrolytic enzyme alkaline phosphatase were...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
The phosphate regulation and subcellular location of the hydrolytic enzyme alkaline phosphatase were...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1), whose activity sur...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
Cell-free preparations of Proteus mirabilis contained a phosphatase (EC 3.1.3.1) whose activity surp...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 ...
The phosphate regulation and subcellular location of the hydrolytic enzyme alkaline phosphatase were...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...
The phosphatase activities of cells of representative enterobacterial species were studied after cel...