Results 201 to 210 of about 29,854 (231)
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2019
The method of obtaining and purification of recombinant chaperon GroEL (prokaryotic homolog of eukaryotic chaperon Hsp60) including the protein expression in E. coli cells, precipitation with saturated ammonium sulphate from a producent lysate, gel-filtration on Sephacryl-300 column and ion-exchange chromatography on MonoQ HR 5/5 column, is described ...
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The method of obtaining and purification of recombinant chaperon GroEL (prokaryotic homolog of eukaryotic chaperon Hsp60) including the protein expression in E. coli cells, precipitation with saturated ammonium sulphate from a producent lysate, gel-filtration on Sephacryl-300 column and ion-exchange chromatography on MonoQ HR 5/5 column, is described ...
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Characterization of the chaperonin GroEL in Mycoplasma gallisepticum
Archives of Microbiology, 2014Mycoplasma gallisepticum (MG) is a common and widespread cause of chronic respiratory disease in poultry. In this study, antigenic proteins were identified from MG membrane using two-dimensional gel electrophoresis (2-DE) analysis followed by Western blot and matrix-assisted desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS ...
Lei, Tan +9 more
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Oxidized GroEL can function as a chaperonin
Frontiers in Bioscience, 2004Here, we report on the facilitated reactivation (85%) of oxidatively inactivated rhodanese by an oxidized form of the molecular chaperone GroEL (ox-GroEL). Reactivation by ox-GroEL required a reductant, and the enzyme substrate, sodium thiosulfate.
Girish C, Melkani +2 more
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Immunodetection of the recombinant GroEL by the Nanobody NbBruc02
World Journal of Microbiology and Biotechnology, 2012Brucella has a great impact on health and economy in Syria, thus much effort is being placed on the development of diagnostics and vaccines. In this context, a wide Nanobody "immune" library was previously established, from which several Brucella-specific binders were isolated.
Lubna, Abo Assali +3 more
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A biochemical screen for GroEL/GroES inhibitors
Bioorganic & Medicinal Chemistry Letters, 2014High-throughput screening of 700,000 small molecules has identified 235 inhibitors of the GroEL/GroES-mediated refolding cycle. Dose-response analysis of a subset of these hits revealed that 21 compounds are potent inhibitors of GroEL/GroES-mediated refolding (IC50
Steven M, Johnson +8 more
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Refolding of Denatured Trichosanthin in the Presence of GroEL
Biochemical and Biophysical Research Communications, 1998The stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating protein, was investigated in the presence of guanidinium chloride (GdnHCl). The process of unfolding was monitored by CD and fluorescence spectroscopy. Both methods show the presence of partially folded intermediates. Unfolding of TCS is attained in 6M GdnHCl, but the inactive species
C K, Lau, R N, Wong, S C, Lo, F, Kwok
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Basis of Substrate Binding by the Chaperonin GroEL
Biochemistry, 1999The molecular chaperonins are essential proteins involved in protein folding, complex assembly, and polypeptide translocation. While there is abundant structural information about the machinery and the mechanistic details of its action are well studied, it is yet unresolved how chaperonins recognize a large number of structurally unrelated polypeptides
Z, Wang +4 more
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Mechanism of substrate recognition by the chaperonin GroEL
Biochemistry and Cell Biology, 2001The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroELGroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm. The chaperonin facilitates protein folding by enclosing substrate proteins in a cage defined by the GroEL cylinder ...
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Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL
MBio, 2021Jared Sivinski +2 more
exaly
Lactobacillus stress protein GroEL prevents colonic inflammation
Journal of Gastroenterology, 2021François Hermetet +2 more
exaly

