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Methylglyoxal

About: Methylglyoxal is a research topic. Over the lifetime, 2844 publications have been published within this topic receiving 102037 citations. The topic is also known as: acetylformaldehyde & pyruvaldehyde.


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Journal ArticleDOI
15 Aug 1976
TL;DR: In this article, the time-resolved fluorescence of methyl glyoxal was studied as a function of excitation energy and pressure, and a dual fluorescence was observed in all circumstances, and from these measurements the parameters describing the singlet-triplet coupling, the disspative leak rates from singlet and triplet states and the fluorescence quenching constants.
Abstract: The time-resolved fluorescence of methylglyoxal was studied as a function of excitation energy and pressure. In all circumstances a dual fluorescence was observed. From these measurements was obtained the parameters describing the singlet-triplet coupling, the disspative leak rates from singlet and triplet states and the fluorescence quenching constants. Also, the pressure induction of the thermalized phosphorescence was studied. As found previously in biacetyl, the excited manifold should be divided into a black note region and an overlap region, the former being more extensive in methylglyoxal. The decal characteristics of methylglyoxal are intermediate between those of glyoxal and biacetyl. The differences in behavior between the three molecules can be readily understood on the basis of the differences in their level densities, due to the different number of atoms in these molecules.

34 citations

Journal ArticleDOI
TL;DR: In this article, a separation system for N e -(carboxyethyl)lysine (CEL) was developed by HPLC equipped with a styrene-divinylbenzene copolymer resin coupled with sulfonic group cation-exchange column and examined whether CEL is formed from proteins modified by glucose via the Maillard reaction.

34 citations

Journal ArticleDOI
TL;DR: In this article, a comparative study of the ability of MG detoxification of these three enzymes has been done in both E. coli and yeast in presence of different abiotic stress revealed the contribution of each of these genes in detoxifying MG.
Abstract: Methylglyoxal(MG) is a potent cytotoxin that is produced as a byproduct of various metabolic reactions in the cell. The major enzymes for MG detoxification are Glyoxalase I(GLYI), Glyoxalase II(GLYII) and D-lactate dehydrogenase(D-LDH). These three enzymes work together and convert MG into D-pyruvate, which directly goes to TCA cycle. Here, a comparative study of the ability of MG detoxification of these three enzymes has been done in both E. coli and yeast. Ectopic expression of these three genes from Arabidopsis in E. coli in presence of different abiotic stress revealed the contribution of each of these genes in detoxifying MG. Yeast mutants of MG detoxification enzymes were also grown in different stress conditions to record the effect of each gene. These mutants were also used for complementation assays using the respective MG detoxifying genes from Arabidopsis in presence of various stress conditions. The MG content and the corresponding growth of cells was measured in all the bacterial as well as yeast strains. This study reveals differential contribution of MG detoxification enzymes in mitigating MG levels and alleviating stress in both prokaryotes as well as eukaryotes. GLYI and D-LDH were found to be key enzymes in MG detoxification under various abiotic stresses.

34 citations

Journal ArticleDOI
TL;DR: Methylglyoxal strongly inhibited the glycolaldehyde activity of the E1 and E2 isozymes, respectively, and mixed-type models of inhibition were employed as an approach to calculate the inhibition constants.
Abstract: Methylglyoxal was demonstrated to be a substrate for the isozymes E1, E2 and E3 of human aldehyde dehydrogenase. Pyruvate was the product from the oxidation of methylglyoxal by the three isozymes. At pH 7.4 and 25 degrees C, the major and minor components of the E3 isozyme catalyzed the reaction with Vmax of 1.1 and 0.8 mumol NADH min-1 mg-1 protein, respectively, compared to 0.067 and 0.060 mumol NADH min-1 mg-1 protein for the E1 and E2 isozymes, respectively. The E2 isozyme had a K(m) for methylglyoxal of 8.6 microM, the lowest compared to 46 microM for E1 and 586 and 552 microM for the major and minor components of the E3 isozyme, respectively. Both components of the E3 isozyme showed substrate inhibition by methylglyoxal, with Ki values of 2.0 mM for the major component and 12 mM for the minor component at pH 9.0. Substrate inhibition by methylglyoxal was not observed with the E1 and E2 isozymes. Methylglyoxal strongly inhibited the glycolaldehyde activity of the E1 and E2 isozymes. Mixed-type models of inhibition were employed as an approach to calculate the inhibition constants, 44 and 10.6 microM for E1 and E2 isozymes, respectively.

34 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023112
2022306
2021173
2020156
2019153
2018128