The Use of HPLC for the Purification of the Qв-Protein

1987 ◽  
Vol 42 (6) ◽  
pp. 739-741 ◽  
Author(s):  
Günter F. Wildner ◽  
Claudia Fiebig ◽  
Norbert Dedner ◽  
H. E. Meyer
Keyword(s):  
Photosystem Ii ◽  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Reversed Phase ◽  
Reversed Phase Chromatography ◽  
Linear Gradient ◽  
Photoaffinity Label ◽  
Reaction Center Complex ◽  
Peak Fraction ◽  
Second Peak

The Qв-protein is as a hydrophobic integral membrane protein firmly bound in the reaction center complex of photosystem II. A new method was developed to purify the SDS extracted protein using reversed-phase chromatography with two binary linear gradient systems. The identification of the Qв-protein was achieved by its rapidly labeling during photoassimilation of [35S]sulfate and by its reaction with the photoaffinity label azido-[14C]atrazine. Furtherm ore, antisera against the purified Qв-protein reacted with a single peak fraction, the second peak of the chrom atogram , which was identical with the labeled protein peak fraction.

High-performance liquid chromatography of pyruvic and alpha-ketoglutaric acids and its application to urine samples.

1977 ◽  
Vol 23 (5) ◽  
pp. 802-805 ◽  
Author(s):  
J C Liao ◽  
N E Hoffman ◽  
J J Barboriak ◽  
D A Roth
Keyword(s):  
Aqueous Solution ◽  
High Performance Liquid Chromatography ◽  
High Performance ◽  
Ammonium Acetate ◽  
Gradient Elution ◽  
Reversed Phase ◽  
Diabetic Patients ◽  
Reversed Phase Chromatography ◽  
Linear Gradient ◽  
Normal Individuals

Abstract Pyruvic and alpha-ketoglutaric acids were quantitatively and rapidly converted to quinoxalones by a new method, to enhance their detectability in the ultraviolet. The quinoxalones were separated by reversed-phase chromatography with use of 10 micronm particles packed in a 30-cm (length) column. An aqueous solution of ammonium acetate and methanol was used for linear gradient elution. The urinary excretion of pyruvic and alpha-ketoglutaric acids by normal individuals, diabetic patients, and patients with renal dysfunction was determined.

scholarly journals Predicting the Structure and Dynamics of Membrane Protein GerAB from Bacillus subtilis

2021 ◽  
Vol 22 (7) ◽  
pp. 3793
Author(s):  
Sophie Blinker ◽  
Jocelyne Vreede ◽  
Peter Setlow ◽  
Stanley Brul
Keyword(s):  
Bacillus Subtilis ◽  
Membrane Protein ◽  
Spore Germination ◽  
Structural Information ◽  
Transmembrane Protein ◽  
Homology Modelling ◽  
Water Channel ◽  
Md Simulations ◽  
Integral Membrane Protein ◽  
Starting Point

Bacillus subtilis forms dormant spores upon nutrient depletion. Germinant receptors (GRs) in spore’s inner membrane respond to ligands such as L-alanine, and trigger spore germination. In B. subtilis spores, GerA is the major GR, and has three subunits, GerAA, GerAB, and GerAC. L-Alanine activation of GerA requires all three subunits, but which binds L-alanine is unknown. To date, how GRs trigger germination is unknown, in particular due to lack of detailed structural information about B subunits. Using homology modelling with molecular dynamics (MD) simulations, we present structural predictions for the integral membrane protein GerAB. These predictions indicate that GerAB is an α-helical transmembrane protein containing a water channel. The MD simulations with free L-alanine show that alanine binds transiently to specific sites on GerAB. These results provide a starting point for unraveling the mechanism of L-alanine mediated signaling by GerAB, which may facilitate early events in spore germination.

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