Characterization of Escherichia coli expressing an Lpp’OmpA(46-159)-PhoA fusion protein localized in the outer membrane

1996 ◽  
Vol 45 (1-2) ◽  
pp. 112-119 ◽  
Author(s):  
C. Stathopoulos ◽  
G. Georgiou ◽  
C. F. Earhart
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Outer Membrane ◽  
Phoa Fusion

Expression, purification, and characterization of a novel recombinant fusion protein, rhTPO/SCF, in Escherichia coli

2006 ◽  
Vol 47 (2) ◽  
pp. 427-433 ◽  
Author(s):  
Yuhui Zang ◽  
Xu Zhang ◽  
Dawen Yuan ◽  
Yumin Zhang ◽  
Jie Zhu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Recombinant Fusion Protein ◽  
Purification And Characterization

scholarly journals Molecular and Biochemical Characterization of the xlnD-Encoded 3-Hydroxybenzoate 6-Hydroxylase Involved in the Degradation of 2,5-Xylenol via the Gentisate Pathway in Pseudomonas alcaligenes NCIMB 9867

2005 ◽  
Vol 187 (22) ◽  
pp. 7696-7702 ◽  
Author(s):  
Xiaoli Gao ◽  
Chew Ling Tan ◽  
Chew Chieng Yeo ◽  
Chit Laa Poh
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Molecular Mass ◽  
Electron Donor ◽  
Biochemical Characterization ◽  
Aromatic Substrates ◽  
Gentisate Pathway ◽  
A Subunit ◽  
Pseudomonas Alcaligenes

ABSTRACT The xlnD gene from Pseudomonas alcaligenes NCIMB 9867 (strain P25X) was shown to encode 3-hydroxybenzoate 6-hydroxylase I, the enzyme that catalyzes the NADH-dependent conversion of 3-hydroxybenzoate to gentisate. Active recombinant XlnD was purified as a hexahistidine fusion protein from Escherichia coli, had an estimated molecular mass of 130 kDa, and is probably a trimeric protein with a subunit mass of 43 kDa. This is in contrast to the monomeric nature of the few 3-hydroxybenzoate 6-hydroxylases that have been characterized thus far. Like other 3-hydroxybenzoate 6-hydroxylases, XlnD could utilize either NADH or NADPH as the electron donor. P25X harbors a second 3-hydroxybenzoate 6-hydroxylase II that was strictly inducible by specific aromatic substrates. However, the degradation of 2,5-xylenol and 3,5-xylenol in strain P25X was found to be dependent on the xlnD-encoded 6-hydroxylase I and not the second, strictly inducible 6-hydroxylase II.

Expression, refolding, and characterization of recombinant thrombopoietin/stem cell factor fusion protein in Escherichia coli

2007 ◽  
Vol 74 (4) ◽  
pp. 836-842 ◽  
Author(s):  
Yuhui Zang ◽  
Xu Zhang ◽  
Xiaoling Jiang ◽  
Haoran Li ◽  
Jie Zhu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stem Cell ◽  
Fusion Protein ◽  
Stem Cell Factor

Isolation and characterization of two outer membrane preparations from Escherichia coli

1975 ◽  
Vol 375 (1) ◽  
pp. 44-53 ◽  
Author(s):  
Shoji Mizushima ◽  
Hisami Yamada
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Isolation And Characterization

scholarly journals Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components

Microbiology ◽  
2006 ◽  
Vol 152 (8) ◽  
pp. 2405-2420 ◽  
Author(s):  
Anu Daniel ◽  
Aparna Singh ◽  
Lynette J. Crowther ◽  
Paula J. Fernandes ◽  
Wiebke Schreiber ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Cytoplasmic Membrane ◽  
Complete Characterization ◽  
Type Iv Pili ◽  
Amino Terminus ◽  
Type Iv ◽  
Membrane Components ◽  
Nucleotide Binding Proteins

Typical enteropathogenic Escherichia coli strains express an established virulence factor belonging to the type IV pili family, called the bundle-forming pilus (BFP). BFP are present on the cell surface as bundled filamentous appendages, and are assembled and retracted by proteins encoded by the bfp operon. These proteins assemble to form a molecular machine. The BFP machine may be conceptually divided into three components: the cytoplasmic membrane (CM) subassembly, which is composed of CM proteins and cytoplasmic nucleotide-binding proteins; the outer membrane (OM) subassembly and the pilus itself. The authors have previously characterized the CM subassembly and the pilus. In this study, a more complete characterization of the OM subassembly was carried out using a combination of biochemical, biophysical and genetic approaches. It is reported that targeting of BfpG to the OM was influenced by the secretin BfpB. BfpG and BfpU interacted with the amino terminus of BfpB. BfpU had a complex cellular distribution pattern and, along with BfpB and BfpG, was part of the OM subassembly.

Kinetic characterization of Escherichia coli outer membrane phospholipase A using mixed detergent-lipid micelles

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1139-1147 ◽  
Author(s):  
Anton J. G. Horrevoets ◽  
Tilman M. Hackeng ◽  
Hubertus M. Verheij ◽  
Ruud Dijkman ◽  
Gerard H. De Haas
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Phospholipase A ◽  
Kinetic Characterization ◽  
Outer Membrane Phospholipase A ◽  
Lipid Micelles

scholarly journals Isolation and characterization of the outer membrane of Escherichia coli with autodisplayed Z-domains

2015 ◽  
Vol 1848 (3) ◽  
pp. 842-847 ◽  
Author(s):  
Min Park ◽  
Gu Yoo ◽  
Ji-Hong Bong ◽  
Joachim Jose ◽  
Min-Jung Kang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Isolation And Characterization
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