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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation01:22

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...

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Related Experiment Video

Updated: Jun 28, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells
11:56

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

Ascorbic acid reaction with disulphide compounds: effects and applications.

W L Baker1

  • 1School of Engineering and Science, Swinburne University of Technology, John Street, PO Box 218, Hawthorn, Vic. 3122, Australia.

Talanta
|October 31, 2008
PubMed
Summary
This summary is machine-generated.

This study presents a new method for quantifying cystine using ascorbic acid and copper. The assay is sensitive to disulphide compounds, which inhibit hydrogen peroxide formation.

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Area of Science:

  • Biochemistry
  • Analytical Chemistry

Background:

  • Cystine, an oxidized amino acid, plays a role in protein structure and various biological processes.
  • Accurate quantification of cystine and other disulphide compounds is crucial for biochemical and clinical analyses.

Purpose of the Study:

  • To develop and validate a novel method for estimating cystine concentrations.
  • To investigate the influence of disulphide compounds, including cystine, glutathione disulphide, and proteins, on the developed assay.

Main Methods:

  • A quantitative method was established utilizing the reaction between cystine, ascorbic acid, and copper ions.
  • A standard curve was generated to measure hydrogen peroxide production.
  • The assay's response to various disulphide compounds was evaluated.

Main Results:

  • The developed method accurately estimates cystine concentrations.
  • Disulphide compounds, such as cystine and glutathione disulphide, were found to reduce hydrogen peroxide formation.
  • These disulphide compounds also decreased the amount of deoxyribose reacting material during ascorbic acid oxidation.

Conclusions:

  • The described reaction provides a reliable basis for estimating cystine levels.
  • The assay's sensitivity to disulphide compounds allows for their detection and potential quantification in biological samples.
  • This method is applicable for determining disulphide amino acid content in protein hydrolysates.