Journal ArticleDOI
Thiol groups in proteins as endogenous reductants to determine glutathione-protein mixed disulphides in biological systems
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TLDR
The basal GSSP content determined in rat liver, heart, lung, testis, spleen and brain corresponded to that reported in the literature and determined by more complex sample preparation or labor-intensive analytical procedures.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1995-02-23. It has received 77 citations till now. The article focuses on the topics: Glutathione.read more
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Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery
TL;DR: This Review will focus exclusively on cysteine, whose identity as cellular target or “sensor” of reactive intermediates is most prevalent and established and which results in a range of sulfur-containing products, not just disulfide bridges, as typically presented in biochemistry textbooks.
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Effect of fish meal replacement by plant protein sources on non-specific defence mechanisms and oxidative stress in gilthead sea bream (Sparus aurata)
Ariadna Sitjà-Bobadilla,Samuel Peña-Llopis,Pedro Gómez-Requeni,Françoise Médale,Sadasivam Kaushik,Jaume Pérez-Sánchez +5 more
TL;DR: Partial or total replacement of fish meal by a mixture of plant protein (PP) sources (corn gluten, wheat gluten, extruded peas, rapeseed meal and sweet white lupin) balanced with indispensable amino acids was examined in juvenile gilthead sea bream over the course of a 6-month growth trial as mentioned in this paper.
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Molecular mechanisms and potential clinical significance of S-glutathionylation.
Isabella Dalle-Donne,Aldo Milzani,Nicoletta Gagliano,Roberto Colombo,Daniela Giustarini,Ranieri Rossi +5 more
TL;DR: Much investigation is needed to clarify the actual involvement of protein S-glutathionylation in many human diseases, because of the redox potential of most Cys residues and the GSSG export by most cells as a protective mechanism against oxidative stress.
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Effects of age and caloric restriction on glutathione redox state in mice.
TL;DR: Results suggest that the aging process in the mouse is associated with a gradual pro-oxidizing shift in the glutathione redox state and that CR attenuates this shift.
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Protein glutathionylation in health and disease.
TL;DR: This review underlines the peculiarities of this post-translational modification and their biological role and identifies two major open problems in the field, namely the complexity of the mechanisms responsible for glutathionylation and de-glutathionyation, as well as what makes a protein susceptible to glutath ionylation.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides.
TL;DR: A rapid and sensitive high-performance liquid chromatography method for determination of nanomole levels of glutathione, glutathiona disulfide, cysteine glutathion-mixed disulfides and 20 related sulfur-containing amino acids or their derivatives has been described.
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Denatured States of Proteins
Ken A. Dill,David Shortle +1 more
TL;DR: The development of synthetic, peptide and protein fragment models of the denatured state and the recent progress in NMR spectroscopy provide bases for optimism that new insights will be gained into this poorly understood realm of protein biochemistry.
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Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
TL;DR: EnzYMES MODIFIED BY THIOL : DISULFIDE EXCHANGE-AN OVERVIEW .