OXIDATION OF CITRATE ISOCITRATE + CIS-ACONITATE BY ISOLATED MITOCHONDRIA
OXIDATION OF CITRATE ISOCITRATE + CIS-ACONITATE BY ISOLATED MITOCHONDRIA
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DOI:
10.1042/bj0900225
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发表时间:
1964-01-01
影响因子:
4.1
通讯作者:
CHAPPELL, JB
中科院分区:
文献类型:
--
作者:
CHAPPELL, JB
The oxidation of Ls (+)-isocitrate by isolated mitochondria was in-vestigated. In mitochondria depleted of their endogenous substrates by preincubation with adenosine diphosphate together with phosphate or dinitrophenol, isocitrate was no oxidized at significant rates, until malate, oxaloacetate or fumarate was added in catalytic amounts. In the presence of [beta]-chlorovinylarsenious oxide or malonate, which inhibit the production of malate from isocitrate, the addition of the above-named dicarboxylic acids was necessary before isocitrate was oxidized. With mitochondria that were depleted of their endo-genous substrates, extensive reduction of intramitochondrial nico-tinamide nucleotide, consistent with active respiration, was obtained only when both isocitrate and malate were added together. The nicotinamideadenine dinucleotide phosphate reduced by the isocitrate dehydrogenase is re-oxidized by nicotinamide nucleotide transhydro-genase and malate dehydrogenase. Citrate was oxidized at a rate 40-60% of that of isocitrate and cis-aconitate. It is suggested that this is due to a relatively low aconitase activity. These findings were discussed in relation to the morphology of the mitochondrion.