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mirabilis jalapa/phosphatase

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[Phosphatase from Proteus mirabilis].

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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
The uropathogenic Gram-negative bacterium Proteus mirabilis exhibits a form of multicellular behaviour termed swarming, which involves cyclical differentiation of typical vegetative cells into filamentous, multinucleate, hyperflagellate swarm cells capable of rapid and co-ordinated population

Proteus mirabilis urease: transcriptional regulation by UreR.

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Proteus mirabilis urease catalyzes the hydrolysis of urea, initiating the formation of urinary stones. The enzyme is critical for kidney colonization and the development of acute pyelonephritis. Urease is induced by urea and is not controlled by the nitrogen regulatory system (ntr) or catabolite

[Isolation and purification of restriction endonuclease PmiI from Proteus mirabilis 1667].

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A new restriction endonuclease Pmi I was detected in Proteus mirabilis 1667. The enzyme hydrolyzes DNA of the phage lambda into 10 electrophoretically separating fragments with molecular weights of 1.3-7.9 mD. With the use of two-stage chromatography on blue sepharose and phosphocellulose it is

Two new naphthalene glucosides and other bioactive compounds from the carnivorous plant Nepenthes mirabilis.

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Two new naphthalene diglucosides named nepenthosides A (1) and B (2), together with eleven known compounds (3-13), were isolated from the carnivorous plant Nepenthes mirabilis. The structures of these compounds were elucidated based on extensive spectroscopic analysis, including 1D- and 2D-NMR, and
Proteus mirabilis is a ubiquitous bacterium associated with complicated urinary tract infection (UTI). Mutagenesis studies of the wild-type strain HI4320 in the CBA mouse model of ascending UTIs have identified attenuated mutants with transposon insertions in genes encoding the high-affinity
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