Isolation and purification of recombinant serine/threonine protein kinases of the strain Bifidobacterium longum B379M and investigation of their activity

Previously, we identified six serine/threonine protein kinases (STPK) of Bifidobacterium and named them Pkb1–Pkb6. In the present study, we optimized methods for isolation of the six STPK catalytic domains proteins of B. longum B379M: a method for isolation of Pkb3 and Pkb4 in native conditions, a m...

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Veröffentlicht in:	Biochemistry (Moscow) 2015-10, Vol.80 (10), p.1303-1311
Hauptverfasser:	Alekseeva, M. G., Mavletova, D. A., Kolchina, N. V., Nezametdinova, V. Z., Danilenko, V. N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial proteins Bifidobacterium Bifidobacterium - enzymology Bifidobacterium - genetics Bifidobacterium longum Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Catalytic Domain Culture Techniques Dialysis Escherichia coli - cytology Escherichia coli - genetics Escherichia coli - growth & development Inclusion Bodies - genetics Kinases Life Sciences Microbiology Observations Phosphorylation Physiological aspects Protein kinases Protein-protein interactions Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - isolation & purification Protein-Serine-Threonine Kinases - metabolism Proteins Recombinant proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Solubility
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