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Purification and characterization of NADPH-dependent 2-oxoaldehyde reductase from porcine liver. A self-defence enzyme preventing the advanced stage of the Maillard reaction
- Source :
- European Journal of Biochemistry. 197:373-379
- Publication Year :
- 1991
- Publisher :
- Wiley, 1991.
-
Abstract
- An enzyme which catalyzes the reduction of 3-deoxyglucosone to 3-deoxyfructose and methylglyoxal to acetol, was isolated and purified from porcine liver. 2-Oxoaldehyde compounds were found to be especially good substrates and monocarbonyl compounds were poor substrates for this reductase. The optimum pH of the enzyme activity was 6.5. The Km for 3-deoxyglucosone and methylglyoxal were 2.1 mM and 3.3 mM, respectively. The enzyme consisted of a single polypeptide chain with a molecular mass of 38 kDa. The activity of the enzyme was completely inhibited by p-chloromercuribenzoate. The enzyme inhibited the advanced stage of the Maillard reaction.
- Subjects :
- Hot Temperature
Magnetic Resonance Spectroscopy
Swine
Reductase
Biochemistry
Chromatography, DEAE-Cellulose
symbols.namesake
chemistry.chemical_compound
Porcine liver
Animals
Amino Acids
Chromatography, High Pressure Liquid
chemistry.chemical_classification
Molecular mass
biology
Chemistry
Advanced stage
Methylglyoxal
Hydrogen-Ion Concentration
Enzyme assay
Maillard Reaction
Alcohol Oxidoreductases
Kinetics
Maillard reaction
Enzyme
Liver
symbols
biology.protein
Electrophoresis, Polyacrylamide Gel
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 197
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....05f5d949aae845f161302a94740e4935