As judged from oxygen consumption, lung cell mitochondria oxidized glycerol 1 phosphate at a rate (30 to 35 nmoles of oxygen per min per mg protein) comparable to that of 2 oxoglutarate or 50 to 60% of that of succinate. Oxidation of 3 hydroxybutyrate in lung cell mitochondria was slow (6 to 8 nmoles of oxygen per min per mg protein) and corresponded to 20% of that of 2 oxoglutarate or 10% of that of succinate. The significance of oxidation of glycerol 1 phosphate in lung cell mitochondria may reside not only in transfer of cytoplasmic reducing equivalents to mitochondria but also in increased availability of phospholipids for oxidation and coupled energy production. The slow oxidation of 3 hydroxybutyrate might be related to either lack of required enzymatic apparatus or inhibition of the apparatus by fatty acid oxidation.
|Original language||English (US)|
|Title of host publication||AMER.REV.RESP.DIS.|
|Number of pages||3|
|State||Published - 1974|
ASJC Scopus subject areas