Effect of 2,3-butanedione on human myeloperoxidase.
1. Myeloperoxidase is inhibited by various diketones that are recognized arginine reagents. 2. Although arginine residues in the enzyme were modified in both the light and the dark, enzyme inactivation occurred only in the presence of light. 3. Under conditions where diketones caused inactivation of myeloperoxidase, spectral studies indicated marked damage to the haem residues of the enzyme. 4. It was concluded that diketones serve simply as photosensitizers of visible light-induced inactivation of myeloperoxidase. 5. Studies on other haemoproteins indicated the great ease with which the presence of diketones sensitized haem residues for photodestruction.
Willassen
N P
NP
Institute of Medical Biology, University of Tromsø, Norway.
Little
C
C
D000596:Amino Acids / Q000032:analysis; D002074:Butanones / Q000494:pharmacology*; D003512:Cyclohexanones / Q000494:pharmacology; D003931:Diacetyl / Q000494:pharmacology*; D006420:Hemeproteins / Q000032:analysis; D006801:Humans; D009195:Peroxidase / Q000037:antagonists & inhibitors* / Q000097:blood; D010658:Phenylglyoxal / Q000494:pharmacology
D000596:Amino Acids; D002074:Butanones; D003512:Cyclohexanones; D006420:Hemeproteins; C018031:1,2-cyclohexanedione; D009195:Peroxidase; D003931:Diacetyl; D010658:Phenylglyoxal