Effects of Carnosine and Related Compounds on Monosaccharide Autoxidation and $H_2O_2$ Formation

  • Lee, Beom-Jun (Laboratory of Veterinary Public Health, College of Veterinary Medicine, Seoul National University) ;
  • Kang, Kyung-Sun (Laboratory of Veterinary Public Health, College of Veterinary Medicine, Seoul National University) ;
  • Nam, Sang-Yoon (Laboratory of Veterinary Public Health, College of Veterinary Medicine, Seoul National University) ;
  • Park, Jae-Hak (Laboratory Animal Medicine, College of Veterinary Medicine, Seoul National University) ;
  • Lee, Yong-Soon (Laboratory of Veterinary Public Health, College of Veterinary Medicine, Seoul National University) ;
  • Yun, Young-Won (Department of Veterinary Physiology, College of Veterinary Medicine, Chungbuk National University) ;
  • Cho, Myung-Haing (Laboratory of Toxicology, College of Veterinary Medicine, Seoul National University)
  • Published : 1999.06.21

Abstract

The effects of carnosine and related compounds (CRCs) including anserine, homocarnosine, histidine, and ${\beta}-alanine$ on monosaccharide autoxidation and $H_2O_2$ formation were investigated. The incubation of CRCs with D-glucose, D-glucosamine, and D, L-glyceraldehyde at $37^{\circ}C$ increased the absorption maxima at 285 nm, 273 nm, and $290{\sim}330$ nm, respectively. D, L-glyceraldehyde was the most reactive sugar with CRCs. The presence of copper strongly stimulated the reaction of carnosine and anserine with D-glucose or D-glucosamine. Carnosine and anserine stimulated $H_2O_2$ formation from D-glucose autoxidation in a dose-dependent manner in the presence of 10 ${\mu}M$ Cu (II). The presence of human serum albumin (HSA) decreased their effect on $H_2O_2$ formation. Carnosine and anserine has a biphasic effect on ${\alpha}-ketoaldehyde$ formation from glucose autoxidation. CRCs inhibited glycation of HSA as determined by hydroxymethyl furfural, lysine residue with free ${\varepsilon}-amino$ group, and fructosamine assay. These results suggest that CRCs may be protective against diabetic complications by reacting with sugars and protecting glycation of protein.

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