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Methods in Enzymology 1977
Topics: Affinity Labels; Fluorescent Dyes; Sulfhydryl Reagents; Thiosulfonic Acids
PubMed: 927196
DOI: 10.1016/0076-6879(77)47042-3 -
Current Protocols in Protein Science Apr 2016The reagents and methods for purification and use of the most commonly used denaturants, guanidine hydrochloride (guanidine-HCl) and urea, are described. Other protein...
The reagents and methods for purification and use of the most commonly used denaturants, guanidine hydrochloride (guanidine-HCl) and urea, are described. Other protein denaturants and reagents used to fold proteins are briefly mentioned. Sulfhydryl reagents (reducing agents) and "oxido-shuffling" (or oxidative regeneration) systems are also described.
Topics: Biochemistry; Guanidine; Indicators and Reagents; Kinetics; Oxidation-Reduction; Protein Denaturation; Protein Folding; Protein Stability; Proteins; Reducing Agents; Solvents; Sulfhydryl Reagents; Urea
PubMed: 27038271
DOI: 10.1002/0471140864.psa03as84 -
Free Radical Biology & Medicine May 2000Mitochondrial oxidative damage and dysfunction contributes to a number of cell pathologies. To investigate how this damage affects cell function we have developed... (Review)
Review
Mitochondrial oxidative damage and dysfunction contributes to a number of cell pathologies. To investigate how this damage affects cell function we have developed mitochondrially targeted antioxidants and thiol reagents by covalently linking them to lipophilic cations. The cation drives the selective accumulation of these reagents into mitochondria within cells where the antioxidants decrease oxidative damage and the thiol reagents enable measurement of the redox status of thiol proteins. In conjunction with cell and animal models of apoptosis, oxidative damage, and nitric oxide signaling, these molecules may provide new insights into the roles of mitochondria in human pathologies.
Topics: Animals; Antioxidants; Cations; Humans; Mitochondria; Mitochondrial Myopathies; Sulfhydryl Reagents
PubMed: 10927180
DOI: 10.1016/s0891-5849(00)00255-0 -
Journal of Bacteriology Aug 1962Schaechter, M. (College of Medicine, University of Florida, Gainesville) and K. Santomassino. Lysis of Escherichia coli by sulfhydryl-binding reagents. J. Bacteriol....
Schaechter, M. (College of Medicine, University of Florida, Gainesville) and K. Santomassino. Lysis of Escherichia coli by sulfhydryl-binding reagents. J. Bacteriol. 84:318-325. 1962-Washed suspensions of gram-negative rods were lysed by low concentrations of some sulfhydryl-binding and oxidizing reagents, but not by reducing agents. Some kinetic aspects of this phenomenon were studied with p-chloromercuribenzoate and Escherichia coli B/r. Structures resulting from the action of this reagent consisted of impure cell walls. These could be purified by treatment with trypsin. Cell walls prepared mechanically and cell membranes obtained by lysing protoplasts were not overtly affected by this chemical.
Topics: Bacteriolysis; Escherichia coli; Indicators and Reagents; Sulfhydryl Compounds; Sulfhydryl Reagents
PubMed: 14497913
DOI: 10.1128/jb.84.2.318-325.1962 -
Biochemistry Mar 1984Glucocorticoid -receptor complexes from intact rat thymus cells incubated with [3H]dexamethasone at 0 degree C are in the nonactivated form and do not bind to...
Glucocorticoid -receptor complexes from intact rat thymus cells incubated with [3H]dexamethasone at 0 degree C are in the nonactivated form and do not bind to DNA-cellulose. Upon being warmed, they are transformed to activated complexes that bind to DNA-cellulose at 0 degree C. We have found that treatment of dexamethasone-receptor complexes with the sulfhydryl-modifying reagents methyl methanethiosulfonate ( MMTS ) and 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), either before or after the warming, inhibits subsequent binding to DNA-cellulose. The effects of these reagents can be reversed at 0 degree C by dithioerythritol and other sulfhydryl-containing compounds. These results provide the first clear evidence that sulfhydryl-modifying reagents inhibit the binding of activated dexamethasone-receptor complexes to DNA-cellulose and suggest that sulfhydryl groups may be located in or near the DNA binding domain of the rat thymus glucocorticoid-receptor complex. Furthermore, addition of dithioerythritol at 0 degree C to nonactivated receptor complexes that have been treated with MMTS or DTNB produces a substantial increase in the capacity of these complexes to bind to DNA-cellulose, raising the possibility that sulfhydryl groups may be associated with a region on the receptor that plays a critical role in the activation process.
Topics: Animals; DNA; Dithioerythritol; Male; Oxidation-Reduction; Protein Binding; Rats; Receptors, Glucocorticoid; Receptors, Steroid; Sulfhydryl Reagents
PubMed: 6722099
DOI: 10.1021/bi00302a009 -
General Pharmacology Jul 1999An overview of the literature concerning the effects of thimerosal is presented. Because of its antibacterial effect, thimerosal is used for a variety of practical... (Review)
Review
An overview of the literature concerning the effects of thimerosal is presented. Because of its antibacterial effect, thimerosal is used for a variety of practical purposes such as antiseptic and preservative. In biomedical studies, thimerosal is used as a sulfhydryl reagent, and as a calcium-mobilizing agent. The ability of thimerosal to act as a sulfhydryl group is related to the presence of mercury. Relatively little study has been devoted to the mechanism of the reaction of thimerosal with the sulfhydryl group; the sulfhydryl reactive capacity is mostly concluded on the basis of inactivation of the effect by dithiothreitol (DTT). Thimersal causes a release of calcium from intracellular stores in many cells types; this is followed by an influx of extracellular calcium. Both InsP3- and ryanodine-sensitive calcium stores may be affected. Studies with permeabilized cells or organelles show that the effect of thimerosal on calcium is dependent on the concentration: low concentrations of thimerosal stimulate calcium release, high concentrations are inhibitory. This dependence is not found in intact cells. Thimerosal may activate or inhibit a number of cell functions. These are often related to the ability to release calcium or with the sulfhydryl reactivity. In platelets, thimerosal causes aggregation, increase of arachidonic acid metabolism, and exocytotic release of serotonin. In neutrophils, thimerosal causes, besides an increase of cytosolic free calcium, an increase of formyl-methionyl-leucyl-phenylalanine (fMLP)-activated leukotriene release, and a modulation of chemotactic migration and exocytosis. At low concentrations, thimerosal induces chemotactic migration of neutrophils, in the absence of other chemoattractants. The effect is also observed with thiosalicylic acid, indicating that the stimulation of migration was due to the thiosalicylic acid moiety of the thimerosal molecule. At higher concentrations, thimerosal causes inhibition of fMLP-activated migration. Low concentrations of thimerosal, but not of thiosalicylic acid, induced exocytotic enzyme release from neutrophils. High concentrations of thimerosal inhibited fMLP-activated exocytosis. The results point to an involvement of calcium mobilization and calcium influx of activation, and reaction with sulfhydryl groups for inhibition.
Topics: Animals; Anti-Infective Agents, Local; Calcium; Cell Physiological Phenomena; Humans; Sulfhydryl Reagents; Thimerosal
PubMed: 10428009
DOI: 10.1016/s0306-3623(98)00258-4 -
Kidney International May 1991The present study was designed to address the reactivity and accessibility of the particular class of sulfhydryl groups involved in the regulatory process of renin...
The present study was designed to address the reactivity and accessibility of the particular class of sulfhydryl groups involved in the regulatory process of renin secretion. Both mercurial (such as P-chloromercuriphenyl sulfonate [PCMPS] and non-mercurial sulfhydryl reagents (for example, 6,6-dithiodinicotinic acid [DTDN]), which very slowly penetrate the cell membrane of intact cells, stimulated renin secretion. The membrane permeant sulfhydryl reagent N-ethylmaleimide had no effect on renin secretion but its membrane impermeant derivative, stilbene maleimide, strongly stimulated secretion. Furthermore, disulfide reducing agents such as dithiothreitol (DTT) had no effect on renin secretion at low concentrations, but strongly inhibited it at high concentrations. Several reagents which are known to primarily deplete cellular reduced glutathione were without effect on renin secretion. The stimulation of renin secretion by PCMPS was rapid in onset, and prevented and reversed by DTT and L-cysteine. Furthermore, the maximal stimulatory effect of PCMPS was not additive to that by diuretics with sulfhydryl reactivity (such as, ethacrynic acid and mersalyl). The stimulatory effect of PCMPS was not affected by diuretics which lack sulfhydryl reactivity (such as, bumetanide and furosemide). These results suggest that sulfhydryl reagents of both with and without diuretic activity stimulate renin secretion by reacting with specific class of sulfhydryl groups which are readily accessible from the extracellular compartment. In addition, these results provide further support the possibility that a sulfhydryl-disulfide interchange in the membrane may play a regulatory role in the renin secretory process.
Topics: 4-Chloromercuribenzenesulfonate; Animals; Cell Membrane; Ethylmaleimide; Kidney Cortex; Rabbits; Renin; Sulfhydryl Reagents
PubMed: 1648645
DOI: 10.1038/ki.1991.109 -
The Journal of Membrane Biology 1983The effect of sulfhydryl reagents on the Na+ permeability mechanisms of toad urinary bladder vesicles was examined. The reagents 5,5'-dithiobis (2-nitrobenzoic acid)...
The effect of sulfhydryl reagents on the Na+ permeability mechanisms of toad urinary bladder vesicles was examined. The reagents 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB), iodosobenzoate, and ethylenimine were able to decrease amiloride-inhibited sodium uptake into vesicles when used at low concentrations. When used at higher concentrations these reagents were able to induce large increases in vesicle Na+ permeability that were not sensitive to amiloride. The reagent p-chloro-mercuribenzene sulfonate was able to induce such leaks even at low concentrations. The reagent N-ethylmaleimide was incapable of substantially affecting vesicle Na+ transport in any way. All of the effects observed could be reversed by removing the reagents from the solution surrounding the vesicles. Our results help explain the varied actions of sulfhydryl reagents on intact epithelial tissue.
Topics: Animals; Biological Transport, Active; Bufo marinus; Cell Membrane; Kinetics; Sodium; Sulfhydryl Reagents; Urinary Bladder
PubMed: 6403711
DOI: 10.1007/BF01870673 -
Virology May 1962
Topics: Sulfhydryl Compounds; Sulfhydryl Reagents; Viruses
PubMed: 13860613
DOI: 10.1016/0042-6822(62)90095-8 -
Analytical Methods : Advancing Methods... Aug 2021As a good substrate, gold has been widely applied in the fields of biological diagnosis and biological analysis. By forming Au-S bonds, self-assembled molecules could...
As a good substrate, gold has been widely applied in the fields of biological diagnosis and biological analysis. By forming Au-S bonds, self-assembled molecules could cause monolayer modification on the gold surface and are further connected with different biomolecules via various functional groups such as -OH, COOH, and NH. In this work, we conducted a comprehensive study on the properties of previously synthesized trithiamantane and its derivatives. The results indicated that these molecules exhibited better stability than single sulfhydryl-modified molecules in air and aquatic environments. After being placed in room temperature for 30 days, the modified chip with trithiamantane derivatives did not change significantly, while a large amount of single sulfhydryl reagents fell off the modified chips. In addition, gold nanoparticles modified with trithioadamantane were also more stable in aqueous solutions than those modified with single sulfhydryl groups. We carried out corresponding application research on gold nanoparticles modified with probe DNA with the two as terminal modification groups. The stability of gold nanoparticles modified by trithiamantane derivatives after long-term storage was better than that of monosulfhydryl-modified products. Overall, these results indicated a good application prospect of this material.
Topics: Gold; Metal Nanoparticles; Sulfhydryl Compounds; Sulfhydryl Reagents; Temperature
PubMed: 34236060
DOI: 10.1039/d1ay00794g