scholarly journals Expression, purification and characterization of the suppressor of copper sensitivity (Scs) B membrane protein from Proteus mirabilis

2022 ◽  
pp. 106047
Author(s):  
Russell J. Jarrott ◽  
Emily J. Furlong ◽  
Guillaume A. Petit ◽  
David Drew ◽  
Jennifer L. Martin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Proteus Mirabilis ◽  
Purification And Characterization

scholarly journals Purification and characterization of three forms of glutathione transferase from Proteus mirabilis

1988 ◽  
Vol 255 (3) ◽  
pp. 971-975 ◽  
Author(s):  
C Di Ilio ◽  
A Aceto ◽  
R Piccolomini ◽  
N Allocati ◽  
A Faraone ◽  
...  
Keyword(s):  
Amino Acid ◽  
Isoelectric Focusing ◽  
Proteus Mirabilis ◽  
Gel Electrophoresis ◽  
Glutathione Transferase ◽  
Total Activity ◽  
Purification And Characterization ◽  
Substrate Specificities ◽  
Structural Differences

Three forms of glutathione transferase (GST) with pI values of 6.0, 6.4 and 7.3 were isolated from Proteus mirabilis AF 2924 by glutathione-affinity chromatography followed by isoelectric focusing, and their structural, kinetic and immunological properties were investigated. Upon SDS/polyacrylamide-slab-gel electrophoresis, all forms proved to be composed of two subunits of identical (22,500) Mr. GST-6.0 and GST-6.4 together account for about 95% of the total activity, whereas GST-7.3 is present only in trace amounts. Extensive similarities have been found between GST-6.0 and GST-6.4. These include subunit molecular mass, amino acid composition, substrate specificities and immunological characteristics. GST-7.3 also cross-reacted (non-identity) with antisera raised against bacterial GST-6.0. None of the antisera raised against a number of human, rat and mouse GSTs cross-reacted with the bacterial enzymes, indicating major structural differences between them and the mammalian GSTs. This conclusion is further supported by c.d. spectra.

Purification and characterization of an immunogenic outer membrane protein of Shigella flexneri 2a

Vaccine ◽  
2009 ◽  
Vol 27 (42) ◽  
pp. 5855-5864 ◽  
Author(s):  
Debasis Pore ◽  
Pinki Chowdhury ◽  
Nibedita Mahata ◽  
Amit Pal ◽  
Shinji Yamasaki ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Shigella Flexneri ◽  
Purification And Characterization ◽  
Shigella Flexneri 2A

scholarly journals High-Level Expression, Single-Step Immunoaffinity Purification and Characterization of Human Tetraspanin Membrane Protein CD81

PLoS ONE ◽  
2008 ◽  
Vol 3 (6) ◽  
pp. e2314 ◽  
Author(s):  
Hidehito Takayama ◽  
Prashen Chelikani ◽  
Philip J. Reeves ◽  
Shuguang Zhang ◽  
H. Gobind Khorana
Keyword(s):  
Membrane Protein ◽  
Single Step ◽  
Purification And Characterization ◽  
High Level Expression ◽  
Immunoaffinity Purification ◽  
High Level

scholarly journals Purification and characterization of an 82-kD membrane protein as a neurite outgrowth factor binding protein: possible involvement of NOF binding protein in axonal outgrowth in developing retina.

1991 ◽  
Vol 112 (2) ◽  
pp. 313-322 ◽  
Author(s):  
H Taniura ◽  
C H Kuo ◽  
Y Hayashi ◽  
N Miki
Keyword(s):  
Membrane Protein ◽  
Neurite Outgrowth ◽  
Binding Protein ◽  
Axonal Outgrowth ◽  
Inhibition Assay ◽  
Retinal Neurons ◽  
Purification And Characterization ◽  
Sds Page ◽  
Doublet Band

Neurite outgrowth factor (NOF) is a glycoprotein isolated from an extract of gizzard that induces neurite outgrowth from cultured retinal or ciliary ganglionic (CG) neurons. We have reported that a glycoprotein of approximately 82 kD solubilized from gizzard muscles binds to NOF (ligand blotting) and inhibits the neurite promoting activity of NOF (inhibition assay). The 82-kD protein (NOF binding protein) was purified from gizzard muscle membranes as a doublet band on SDS-PAGE and a polyclonal antibody was raised against it. An NOF binding protein in developing retina exhibited the same physicochemical properties as that of the gizzard muscle. Quantitative decrease in NOF binding protein in embryonic retinas was observed after day 11 by the inhibition assay, ligand blotting, and immunoblotting, its decrease being parallel with reduction of NOF-induced neurite outgrowth of embryonic retinas. In an immunohistochemical study, the antibody stained only the optic fiber layers of the retinas of 8-d embryos, and this staining was no longer detectable in retinas of 18-d embryos. These results suggest that the 82-kD protein is a novel membrane protein that behaves as an NOF receptor and that the loss of neuritic response of the retinal neurons to NOF reflects a decrease in NOF receptor molecules.

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