KINETIC EVALUATION OF SUBSTRATE SPECIFICITY IN THE GLYOXALASE-I CATALYZED DISPROPORTIONATION OF $alpha$-KETOALDEHYDES.

VanderJagt, David L.; Han, L.B.; Lehman, C.H.

doi:10.2172/4632203

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“…A Glo1 activity assay and blood lysate preparation was performed according to a previously described method [23,24] by monitoring the increase in absorbance at 240 nm due to the formation of S-D-lactoylglutathione for 5 min in a 96-well UV-transparent plate (Greiner BioOne, Germany). The concentration of hemithioacetal used in assay is 1.33 mM according to Van der Jagt et al [25]. Glo2 activity was assayed using spectrophotometry according to a previously described method [24] by monitoring the decrease in absorbance at 240 nm due to the hydrolysis of S-D-lactoylglutathione for 5 min.…”

Section: Animals and Experimental Designmentioning

confidence: 99%

Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus

et al. 2012

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The glyoxalase enzymes catalyse the conversion of reactive glucose metabolites into non-toxic products as a part of the cellular defence system against glycation. This study investigated changes in glyoxalase 1 and glyoxalase 2 activities and the development of diabetic complications in experimental animal models of obesity (Zucker fa/fa rats) and type 2 diabetes mellitus (Goto-Kakizaki rats). In contrast to Zucker rats, in Goto-Kakizaki rats the glyoxalase 1 activities in brain, spinal cord and sciatic nerve tissues were significantly reduced by 10, 32 and 36 %, respectively. Lower glyoxalase 1 activity in the neuronal tissues was associated with a higher blood glucose concentration and impaired endothelium-dependent relaxation to acetylcholine in aortic rings in Goto-Kakizaki rats. This study provides evidence for disturbed neuronal glyoxalase 1 activity under conditions of hyperglycaemia in the presence of impaired endothelium-dependent relaxation and cognitive function.

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