Descriptor: "AprBi" - Searchworks@Jio Institute Digital Library Search Results

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Author: Mikhailova, E. O., Mardanova, A. M., Balaban, N. P., Rudenskaya, G. N., Ilyinskaya, O. N., and Sharipova, M. R.
Subjects: *BACILLUS subtilis, *PROTEINASES, *BACTERIAL growth, *OXIDIZING agents, *CALCIUM ions
Abstract: Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers. [ABSTRACT FROM AUTHOR]
Published: 2009
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Author: Mikhailova E., Mardanova A., Balaban N., Rudenskaya G., Ilyinskaya O., and Sharipova M.
Subjects: Subtilisin-like proteinase, AprBi, Dimers
Abstract: Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H 2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers. © 2009 Pleiades Publishing, Ltd.
Published: 2009

Author: Mikhailova E., Mardanova A., Balaban N., Rudenskaya G., Ilyinskaya O., Sharipova M., Mikhailova E., Mardanova A., Balaban N., Rudenskaya G., Ilyinskaya O., and Sharipova M.
Abstract: Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H 2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers. © 2009 Pleiades Publishing, Ltd.

Author: Mikhailova E., Mardanova A., Balaban N., Rudenskaya G., Ilyinskaya O., Sharipova M., Mikhailova E., Mardanova A., Balaban N., Rudenskaya G., Ilyinskaya O., and Sharipova M.
Abstract: Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H 2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers. © 2009 Pleiades Publishing, Ltd.

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