Phosphatase from Proteus mirabilis | Fosfataza Proteus mirabilis.

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 accumulation of proteins with chitinase activity in the culture media of the parent and mutant Serratia marcescens strain grown in the presence of mitomycin C | Dinamika nakopleniia belkov s khitinaznoi aktivnost'iu v kul'tural'noi zhidkosti mutantnogo shtamma i iskhodnogo shtamma Serratia marcescens v prisutstvii mitomitsina C.

The study of the accumulation pattern of extracellular proteins with chitinase activity in the parent Serratia marcescens strain Bú 211 (ATCC 9986) grown in the presence of mitomycin C and its mutant strain with the constitutive synthesis of chitinases grown in the absence of the inducer showed that chitinase activity appeared in the culture liquids of both strains at the end of the exponential phase (4 h of growth) and reached a maximum in the stationary phase (18-20 h of growth). The analysis of the culture liquids (12 h of growth) by denaturing electrophoresis in PAAG followed by the protein renaturation step revealed the presence of four extracellular proteins with chitinase activity and molecular masses of 21, 38, 52, and 58 kDa

Production of {\pi}+ and K+ mesons in argon-nucleus interactions at 3.2 AGeV

First physics results of the BM@N experiment at the Nuclotron/NICA complex are presented on {\pi}+ and K+ meson production in interactions of an argon beam with fixed targets of C, Al, Cu, Sn and Pb at 3.2 AGeV. Transverse momentum distributions, rapidity spectra and multiplicities of {\pi}+ and K+ mesons are measured. The results are compared with predictions of theoretical models and with other measurements at lower energies.Comment: 29 pages, 20 figure

The BM@N spectrometer at the NICA accelerator complex

BM@N (Baryonic Matter at Nuclotron) is the first experiment operating and taking data at the Nuclotron/NICA ion-accelerating complex.The aim of the BM@N experiment is to study interactions of relativistic heavy-ion beams with fixed targets. We present a technical description of the BM@N spectrometer including all its subsystems.Comment: 34 pages, 47 figures, 6 table

Phosphatase from Proteus mirabilis | Fosfataza Proteus mirabilis.

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

Phosphatase from Proteus mirabilis | Fosfataza Proteus mirabilis.

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

Phosphatase from Proteus mirabilis | Fosfataza Proteus mirabilis.

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 accumulation of proteins with chitinase activity in the culture media of the parent and mutant Serratia marcescens strain grown in the presence of mitomycin C | Dinamika nakopleniia belkov s khitinaznoi aktivnost'iu v kul'tural'noi zhidkosti mutantnogo shtamma i iskhodnogo shtamma Serratia marcescens v prisutstvii mitomitsina C.

The study of the accumulation pattern of extracellular proteins with chitinase activity in the parent Serratia marcescens strain Bú 211 (ATCC 9986) grown in the presence of mitomycin C and its mutant strain with the constitutive synthesis of chitinases grown in the absence of the inducer showed that chitinase activity appeared in the culture liquids of both strains at the end of the exponential phase (4 h of growth) and reached a maximum in the stationary phase (18-20 h of growth). The analysis of the culture liquids (12 h of growth) by denaturing electrophoresis in PAAG followed by the protein renaturation step revealed the presence of four extracellular proteins with chitinase activity and molecular masses of 21, 38, 52, and 58 kDa

Endonuclease from Proteus mirabilis | Endonukleaza Proteus mirabilis.

Two isoforms of nuclease displaying DNase and RNase activities were found in the culture liquid and periplasm of Proteus mirabilis. The enzyme was isolated from the periplasm and then purified to a functionally homogeneous state. The nuclease was equally potent in cleaving denatured and native DNAs by the endonuclease mechanism and was designated Pm endonuclease. The endonuclease was shown to be a temperature-dependent enzyme with a pH optimum of 10.4-10.6, requiring the presence of bivalent metal ions and inhibited by citrate and ethylenediaminetetraacetate