Comparison of protective properties of resveratrol and melatonin in the radiation inactivation and destruction of glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase.

This work investigates the effect of resveratrol and melatonin on structural and functional changes of two enzymes, lactate dehydrogenase (LDH) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), exposed to radiation-induced reactive oxygen species. Solutions of dehydrogenases with or without antioxidants (resveratrol or melatonin) were irradiated with X-rays under the atmosphere of air and at room temperature (21 ± 2 °C). In order to determine the protective effect of melatonin and resveratrol in radiation-induced damage to GAPDH and LDH spectroscopy and HPLC methods were used.

Functional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenase.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the key redox-sensitive proteins whose activity is largely affected by oxidative modifications at its highly reactive cysteine residue in the enzyme's active site (Cys149). Prolonged exposure to oxidative stress may cause, inter alia, the formation of intermolecular disulfide bonds leading to accumulation of GAPDH aggregates and ultimately to cell death. Recently these anomalies have been linked with the pathogenesis of Alzheimer's disease.

Analysis of Potential Binding Sites of 3,5,4'-Trihydroxystilbene (Resveratrol) and trans-3,3',5,5'-Tetrahydroxy-4'-methoxystilbene (THMS) to the GAPDH Molecule Using a Computational Ligand-Docking Method: Structural and Functional Changes in GAPDH Induced by the Examined Polyphenols.

The presented study analyzed potential binding sites of 3,5,4'-trihydroxystilbene (resveratrol, RSV) and its derivative, trans-3,3',5,5'-tetrahydroxy-4'-methoxystilbene (THMS) to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The effects of stilbene analogs on the structure of GAPDH were determined by fluorescence spectroscopy and ζ potential measurements. To what extent the studied compounds affect the activity of the enzyme was also assessed.

Inactivation of chosen dehydrogenases by the products of water radiolysis and secondary albumin and haemoglobin radicals.

Purpose: Inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), alcohol dehydrogenase (ADH) and lactate dehydrogenase (LDH) by products of water radiolysis and by secondary radicals localized on haemoglobin (Hb) and human albumin (HSA) was studied.

Materials And Methods: Aqueous solutions of ADH, GAPDH and LDH were irradiated under air and under nitrous oxide (N2O) in the absence and in the presence of Hb or HSA. In order to determine the effectiveness of inactivation of the enzymes by radicals localized on Hb and HSA, the inactivation efficiency determined experimentally was compared with that calculated under assumption that only hydroxyl radicals are responsible for the enzyme inactivation.

Inactivation of alcohol dehydrogenase (ADH) by ferryl derivatives of human hemoglobin.

In this paper, inactivation of alcohol dehydrogenase (ADH) by products of reactions of H2O2 with metHb has been studied. Inactivation of the enzyme was studied in two systems corresponding to two kinetic stages of the reaction. In the first system H2O2 was added to the mixture of metHb and ADH [the (metHb+ADH)+H2O2] system (ADH was present in the system since the moment of addition of H2O2 i.