Mechanism of asymmetric decarboxylation of α-aryl-α-methylmalonate catalyzed by arylmalonate decarboxylase originated from Alcaligenes bronchisepticus
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Thiol-containing biomolecules, such as cysteine (Cys), homocysteine (Hcy), glutathione (GSH), play crucial roles in maintaining biological systems. For example, elevated levels of Hcy have been implicated as an independent risk factor for tumor invasion and metastasis. Being associated with a wide variety of cancer progressions, there is a significant interest in looking for the fluorescent detection of such thiol species (Cys, Hcy, and GSH) in cancer cells. Various thiol-specific probes have been developed on the basis of different strategies. This review focuses on recent contributions for the fluorescent or colorimetric sensors for thiol-containing amino acids, with special emphasis on the design and application of novel fluorophores for detecting thiol-containing amino acids with higher sensitivity. Keywords: Application, cysteine, fluorescent probe, design, glutathione, homocysteine.
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Thiol-reactive linkers, such as iodoacetyl or maleimide, bound to cross-linked agarose are used to attach cysteine-containing peptides covalently to this resin for use in affinity-purification protocols. It is critical to confirm that the peptide contains a reduced cysteine so that the thiol is available for conjugation to the thiol-reactive linker. The column should be sized appropriately for the amount of peptide to be used and the volume of serum to be processed. Excess binding sites on the column must be blocked with free cysteine before use.
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This paper reports findings of an investigation of the unusual colorimetric change of gold nanoparticles in the presence of thiol-containing amino acids such as homocysteine, cysteine and glutathione. The colorimetric change for homocysteine exhibits a rate that is about two orders of magnitude higher than that for cysteine, and at least five orders of magnitude higher than that for glutathione. The reactivity is effectively reduced or suppressed by the co-existence of either cysteine or glutathione. It is believed that the reactivity involves encapsulation of the particles by the thiol-containing amino acids which is followed by crosslinking at the encapsulating shells. In comparison with cysteine and glutathione, homocysteine has a slower encapsulating rate but a faster crosslinking rate. Implications of the findings of the interfacial encapsulation and crosslinking reactivities of gold nanoparticles to potential nanoparticle-enhanced analytical detection of thiol-containing amino acids are also briefly discussed.
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Porphyrinmaleimides were synthesized and characterized. The thiol-containing amino acid l-cysteine reacted with 58% yield with these porphyrins to form bioconjugate adducts. The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).
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Conference Article| December 01 1978 Reversible Cross-Linking for Cysteine Thiol Groups by Alkanebismethylthiosulphonate Reagents DAVID P. BLOXHAM DAVID P. BLOXHAM 1Department of Biochemistry, University of Southampton, Southampton SO9 3TU, U.K. Search for other works by this author on: This Site PubMed Google Scholar Author and article information Publisher: Portland Press Ltd Online ISSN: 1470-8752 Print ISSN: 0300-5127 © 1978 Biochemical Society1978 Biochem Soc Trans (1978) 6 (6): 1259–1262. https://doi.org/10.1042/bst0061259 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn Email Cite Icon Cite Get Permissions Citation DAVID P. BLOXHAM; Reversible Cross-Linking for Cysteine Thiol Groups by Alkanebismethylthiosulphonate Reagents. Biochem Soc Trans 1 December 1978; 6 (6): 1259–1262. doi: https://doi.org/10.1042/bst0061259 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1978 Biochemical Society1978 Article PDF first page preview Close Modal You do not currently have access to this content.
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