Inhibition of microsomal glucose-6-phosphatase induced by ferrylmyoglobin.
Ferrylmyoglobin (ferrylMb) caused inhibition of microsomal glucose-6-phosphatase (G6Pase) during membrane lipid peroxidation. Butylated hydroxytoluene prevented both the inactivation of G6Pase and the lipid peroxidation. Furthermore, ferrylMb was adsorbed on to the membranes and the membrane proteins polymerized during the lipid peroxidation, suggesting that the inactivation of microsomal G6Pase was due to the disturbance of the membrane structure induced by ferrylMb.
Miura
T
T
Department of Biochemistry, Hokkaido College of Pharmacy, Otaru, Japan.
Muraoka
S
S
Ogiso
T
T
D000818:Animals; D005952:Glucose-6-Phosphatase / Q000037:antagonists & inhibitors*; D015227:Lipid Peroxidation; D008563:Membrane Lipids / Q000378:metabolism; D008786:Metmyoglobin / Q000494:pharmacology*; D008862:Microsomes, Liver / Q000187:drug effects* / Q000201:enzymology; D051381:Rats
D008563:Membrane Lipids; C028048:ferrylmyoglobin; D008786:Metmyoglobin; D005952:Glucose-6-Phosphatase