scholarly journals Inhibition of Urease by Disulfiram, an FDA-Approved Thiol Reagent Used in Humans

Molecules ◽  
2016 ◽  
Vol 21 (12) ◽  
pp. 1628 ◽  
Author(s):  
Ángel Díaz-Sánchez ◽  
Emilio Alvarez-Parrilla ◽  
Alejandro Martínez-Martínez ◽  
Luis Aguirre-Reyes ◽  
Jesica Orozpe-Olvera ◽  
...  
Keyword(s):  
Thiol Reagent

scholarly journals 35S-Cystamine as a Thiol Reagent for the Study of Oxidative Phosphorylation.

1966 ◽  
Vol 20 ◽  
pp. 2629-2632 ◽  
Author(s):  
Sverre Skrede ◽  
A. C. Allison ◽  
C. Lohse ◽  
J. H. Bowie ◽  
D. H. Williams ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Thiol Reagent

scholarly journals The effects of anions on fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli

1981 ◽  
Vol 199 (3) ◽  
pp. 473-477 ◽  
Author(s):  
J J Robinson ◽  
J H Weiner
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Chemical Properties ◽  
Fumarate Reductase ◽  
Maximal Velocity ◽  
Nitrobenzoic Acid ◽  
Thiol Reagent ◽  
Membrane Bound ◽  
Physical And Chemical ◽  
And Chemical Properties

A broad range of anions was shown to stimulate the maximal velocity of purified fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli, while leaving the Km for fumarate unaffected. Reducing agents potentiate the effects of anions on the activity, but have no effect by themselves. Thermal stability, conformation as monitored by circular dichroism and susceptibility to the thiol reagent 5,5′-dithiobis-(2-nitrobenzoic acid) are also altered by anions. The apparent Km for succinate in the reverse reaction (succinate dehydrogenase activity) varies as a function of anion concentration, but the maximal velocity is not affected. The membrane-bound activity is not stimulated by anions and its properties closely resemble those of the purified enzyme in the presence of anions. Thus it appears that anions alter the physical and chemical properties of fumarate reductase, so that it more closely resembles the membrane-bound form.

Cytosolic Ca2+ spikes evoked by the thiol reagent thimerosal in both intact and internally perfused single pancreatic acinar cells

1992 ◽  
Vol 422 (2) ◽  
pp. 173-178 ◽  
Author(s):  
P. Thorn ◽  
P. Brady ◽  
Juan Llopis ◽  
D. V. Gallacher ◽  
O. H. Petersen
Keyword(s):  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Thiol Reagent

scholarly journals The human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein zinc ejection activity of disulfide benzamides and benzisothiazolones: correlation with anti-HIV and virucidal activities.

1997 ◽  
Vol 41 (2) ◽  
pp. 394-400 ◽  
Author(s):  
P J Tummino ◽  
P J Harvey ◽  
T McQuade ◽  
J Domagala ◽  
R Gogliotti ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Antiviral Activity ◽  
Nucleocapsid Protein ◽  
Nitrobenzoic Acid ◽  
Immunodeficiency Virus ◽  
Kinetic Rates ◽  
Thiol Reagent ◽  
Relative Kinetic

It has been shown previously by our group and others that a series of four disulfide benzamides with cellular anti-human immunodeficiency virus (HIV) activity can eject zinc from HIV type 1 nucleocapsid protein (NCp7) in vitro while analogs without antiviral activity do not. We also found that the zinc ejection activity correlates with the loss of the ability of NCp7 to bind to HIV psi RNA in vitro. These observations indicate that the antiviral disulfide benzamides may act at a novel retroviral target of action, i.e., the nucleocapsid protein. The present studies examine the relationship among disulfide benzamide structure, in vitro NCp7 zinc ejection activity, and antiviral activity for a larger series of compounds. All of the antiviral disulfide benzamides were found to eject NCp7 zinc, while some disulfide benzamides with zinc ejection activity are not antiviral. Utilizing the thiol reagent 5,5'-dithiobis(2-nitrobenzoic acid), it was determined that the o-amido-phenyl disulfides being studied cyclize in aqueous solution to form benzisothiazolones. A series of benzisothiazolones, which are stable in solution in the absence of dithiothreitol, were found to eject NCp7 zinc at a rate similar to that of their disulfide benzamide analogs and to possess similar antiviral activity. It was also found that the relative rates of HIV inactivation by various disulfide benzamides and benzisothiazolones correlate with their relative kinetic rates of NCp7 zinc ejection, which is consistent with the nucleocapsid protein being the target of action of these compounds.

scholarly journals Steady-State Kinetics of Enzyme-Catalyzed Hydrolysis of Echothiophate, a P–S Bonded Organophosphorus as Monitored by Spectrofluorimetry

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1371 ◽  
Author(s):  
Irina V. Zueva ◽  
Sofya V. Lushchekina ◽  
David Daudé ◽  
Eric Chabrière ◽  
Patrick Masson
Keyword(s):  
Steady State ◽  
High Efficiency ◽  
High Sensitivity ◽  
High Rate ◽  
Paraoxonase 1 ◽  
Brevundimonas Diminuta ◽  
Steady State Kinetics ◽  
Steady State Kinetic ◽  
Thiol Reagent ◽  
Hydrolysis Of

Enzyme-catalyzed hydrolysis of echothiophate, a P–S bonded organophosphorus (OP) model, was spectrofluorimetrically monitored, using Calbiochem Probe IV as the thiol reagent. OP hydrolases were: the G117H mutant of human butyrylcholinesterase capable of hydrolyzing OPs, and a multiple mutant of Brevundimonas diminuta phosphotriesterase, GG1, designed to hydrolyze a large spectrum of OPs at high rate, including V agents. Molecular modeling of interaction between Probe IV and OP hydrolases (G117H butyrylcholinesterase, GG1, wild types of Brevundimonas diminuta and Sulfolobus solfataricus phosphotriesterases, and human paraoxonase-1) was performed. The high sensitivity of the method allowed steady-state kinetic analysis of echothiophate hydrolysis by highly purified G117H butyrylcholinesterase concentration as low as 0.85 nM. Hydrolysis was michaelian with Km = 0.20 ± 0.03 mM and kcat = 5.4 ± 1.6 min−1. The GG1 phosphotriesterase hydrolyzed echothiophate with a high efficiency (Km = 2.6 ± 0.2 mM; kcat = 53400 min−1). With a kcat/Km = (2.6 ± 1.6) × 107 M−1min−1, GG1 fulfills the required condition of potential catalytic bioscavengers. quantum mechanics/molecular mechanics (QM/MM) and molecular docking indicate that Probe IV does not interact significantly with the selected phosphotriesterases. Moreover, results on G117H mutant show that Probe IV does not inhibit butyrylcholinesterase. Therefore, Probe IV can be recommended for monitoring hydrolysis of P–S bonded OPs by thiol-free OP hydrolases.

scholarly journals Delineation of fucosyltransferase activities with thiol reagents

1979 ◽  
Vol 181 (3) ◽  
pp. 767-769 ◽  
Author(s):  
D Kessel ◽  
T H Chou
Keyword(s):  
Blood Cell ◽  
The Other ◽  
Terminal Galactose ◽  
Thiol Reagent

The thiol reagent dithiothreitol inhibits the activity of a core GDP-fucose-N-acetylglucosaminide alpha-6-fucosyltransferase in plasma and blood-cell homogenates, while promoting the activity of alpha-2- and alpha-3-fucosyltransferases. The latter enzymes catalyse transfer of fucose on to terminal galactose and subterminal N-acetylglucosamine residues respectively. A thiol-blocking reagent N-ethylmaleimide does not affect the activity of the alpha-6-fucosyltransferase, but inhibits the other two enzymes. These results indicate the presence of a critical disulphide linkage in the alpha-6-fucosyltransferase, and provide a means of delineation of different fucosyltransferases.

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