Some derivatives of glutathione

Calam, D.H.; Waley, S. G.

doi:10.1042/bj0850417

Cited by 43 publications

(13 citation statements)

References 7 publications

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“…S-Nitroso-N-acetylpenicillamine (SNAP) was synthesized from Nacetyl-,-penicillamine by the method of Field et al [19]. Glutathione sulphinic acid was synthesized and isolated according to the method described by Calam and Waley [20]. All other chemicals were of reagent grade and were purchased from commercial sources.…”

Section: Methodsmentioning

confidence: 99%

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

Jensen

Belka

Bois

1998

Biochemical Journal

250

209

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An enzyme isolated from rat liver cytosol (native molecular mass 78. 3 kDa; polypeptide molecular mass 42.5 kDa) is capable of catalysing the NADH/NADPH-dependent degradation of S-nitrosoglutathione (GSNO). The activity utilizes 1 mol of coenzyme per mol of GSNO processed. The isolated enzyme has, as well, several characteristics that are unique to alcohol dehydrogenase (ADH) class III isoenzyme: it is capable of catalysing the NAD+-dependent oxidations of octanol (insensitive to inhibition by 4-methylpyrazole), methylcrotyl alcohol (stimulated by added pentanoate) and 12-hydroxydodecanoic acid, and also the NADH/NADPH-dependent reduction of octanal. Methanol and ethanol oxidation activity is minimal. The enzyme has formaldehyde dehydrogenase activity in that it is capable of catalysing the NAD+/NADP+-dependent oxidation of S-hydroxymethylglutathione. Treatment with the arginine-specific reagent phenylglyoxal prevents the pentanoate stimulation of methylcrotyl alcohol oxidation and markedly diminishes the enzymic activity towards octanol, 12-hydroxydodecanoic acid and S-hydroxymethylglutathione; the capacity to catalyse GSNO degradation is also checked. Additionally, limited peptide sequencing indicates 100% correspondence with known ADH class III isoenzyme sequences. Kinetic studies demonstrate that GSNO is an exceptionally active substrate for this enzyme. S-Nitroso-N-acetylpenicillamine and S-nitrosated human serum albumin are not substrates; the activity towards S-nitrosated glutathione mono- and di-ethyl esters is minimal. Product analysis suggests that glutathione sulphinamide is the major stable product of enzymic GSNO processing, with minor yields of GSSG and NH3; GSH, hydroxylamine, nitrite, nitrate and nitric oxide accumulations are minimal. Inclusion of GSH in the reaction mix decreases the yield of the supposed glutathione sulphinamide in favor of GSSG and hydroxylamine.

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Section: Methodsmentioning

confidence: 99%

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

Jensen

Belka

Bois

1998

Biochemical Journal

250

209

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“…GSO 2 H was synthesized by the method of Calam and Waley (15). GSSG (2 mmol) was mixed with 3 mmol of AgNO 3 in 0.2 m NaOAc, pH 6.1, in the dark overnight at room temperature.…”

Section: Hplc Of Gsh and Oxidation Productsmentioning

confidence: 99%

Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro

Yang

et al. 1999

Journal of Lipid Research

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Oxidative modification of LDL may be important in the initiation and/or progression of atherosclerosis, but the precise mechanisms through which low density lipoprotein (LDL) is oxidized are unknown. Recently, evidence for the existence of HOCl-oxidized LDL in human atherosclerotic lesions has been reported, and myeloperoxidase (MPO), which is thought to act through production of HOCl, has been identified in human atherosclerotic lesions. In the present report we describe the formation of 2,4-dinitrophenylhydrazine (DNPH)-reactive modifications in the apolipoprotein (apo) by exposure of LDL to myeloperoxidase in vitro. In contrast with the complex mixture of peptides from oxidation of LDL with reagent HOCl, oxidation with MPO in vitro produced a major tryptic peptide showing absorbance at 365 nm. This peptide was isolated and characterized as VELEVPQL(*C)SFILK . . . , corresponding to amino acid residues 53-66 . . . on apoB-100. Mass spectrometric analyses of two tryptic peptides from oxidation of LDL by HOCl indicated formation of the corresponding methionine sulfoxide (M O), cysteinyl azo (*C), RS-N N-DNP, derivatives of EEL(*C)T(M O)FIR and LNDLNS VLV(M O)PTFHVPFTDLQVPS(*C)K, which suggest oxidation to the corresponding sulfinic acids (RSO 2 H) by HOCl.The present results demonstrate that DNPH-reactive modifications other than aldehydes and ketones can be formed in the oxidation of proteins and illustrate how characterization of specific products of protein oxidation can be useful in assessing the relative contributions of different and unexpected mechanisms to the oxidation of LDL and other target substrates. The data also suggest a direct interaction of the LDL particle with the active site on myeloperoxidase and indicate that effects of the protein microenvironment can greatly influence product formation and stability. -Yang, C-y.,

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“…Glutathione sulphinic acid was prepared according to the method reported earlier (14). -y-Glutamylserylglycine was prepared from reduced glutathione (15).…”

Section: Methodsmentioning

confidence: 99%

⁶⁰Co γ radiolysis of reduced glutathione in aerated solutions at pH values between 1–7.0

Lal¹

1976

Can. J. Chem.

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G-values for the formation of oxidised glutathione (GuS—SGu), glutathione sulphinic acid (GuSO2H), γ-glutamylalanylglycine (GuH), γ-glutamylserylglycine (GuOH), and hydrogen peroxide and G(—GuSH) have been estimated in the γ-radiolysis of aerated reduced glutathione solutions at pH values between 1–7.3. The results show excellent material balance for the radiolytic amino products. Oxygen is necessary for the production of both glutathione sulphinic acid and γ-glutamylserylglycine in the radiolysis of glutathione. Product yields increase with increasing GuSH concentration and reflect the occurrence of a small chain reaction. Although the spectrum of amino products is identical to the corresponding products from cysteine radiolysis under similar conditions, their yields are very much different. It is significant, that there is no evidence for the scission of the peptide chain, at any of the GuSH concentrations and pH's; thus the —SH group of glutathione is the site of attack of the primary species.A reaction mechanism, which explains most of the experimental results has been put forward. A rate expression for G(—GuSH) has been evaluated and it is found that the experimental and calculated G(—GuSH) are in good agreement.

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Some derivatives of glutathione

Cited by 43 publications

References 7 publications

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro

⁶⁰Co γ radiolysis of reduced glutathione in aerated solutions at pH values between 1–7.0

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Some derivatives of glutathione

Cited by 43 publications

References 7 publications

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro

60Co γ radiolysis of reduced glutathione in aerated solutions at pH values between 1–7.0

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⁶⁰Co γ radiolysis of reduced glutathione in aerated solutions at pH values between 1–7.0