Site II-specific inhibition of mitochondrial oxidative phosphorylation by trehalose-6,6′-dimycolate (cord factor) of Mycobacterium tuberculosis
作者： Masahiko Kato
DOI: 10.1016/0003-9861(70)90079-2
关键词:
摘要: Abstract Trehalose-6,6′-dimycolate (cord factor), a toxic glycolipid of Mycobacterium tuberculosis , inhibited the phosphorylation coupled to oxidation either succinate or NADH-linked substrates and caused loss respiratory control in mouse liver mitochondria. Preincubation mitochondrial suspension with cord factor was necessary for this inhibitory action. Liver mitochondria from variety animal species were susceptible action factor. Phosphorylation by ferricyanide (site II phosphorylation) completely damaged, while that associated ascorbate-TMPD III not affected Mycolic acid, alone trehalose, acetylated factor, nontoxic synthetic analog, 6, x -di-(3′-acetoxy, -methoxymycolanoyl)- N -acetyl- d -glucosamine, without effect, two analogs, methyl 6-(3′, -sulphitomycolanoyl)-α- -glucoside 6-(3′-acetoxy, oxidative as did Cord stimulated slightly ATPase. The effect DNP induce ATPase additive. 14 C-labeled firmly bound
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