Abstract
The enzyme, succinic dehydrogenase, was observed to be significantly inhibited by salicylate in in vitro studies(l). A serum salicylate level of 137 mg/100 ml had no effect on hexokinase, cytochrome oxidase or DPNH-cytochrome c reductase(2). In vitro studies with rat liver mitochondria indicated that malate and isocitric dehydrogenase activities were inhibited by salicylate(3,4). An additional study has demonstrated that acetyl salicylic acid fed at levels of 0.005-0.08% of the diet failed to produce a significant difference in growth rate or feed conversion in 3 chick studies(5).
New Hampshire X Delaware chicks were fed 0.3, 0.6 and 0.9% acetyl-salicylic acid (ASA) in addition to the basal diet (Table I). Each dietary treatment was replicated 5 times, and each replicate employed in the experiment consisted of 4 males and 4 females. All chicks were reared for 4 weeks in electrically-heated chick batteries with raised wire floors, and feed and tap water were supplied ad libitum. Feed and body weights were determined for each replicate group at the beginning and end of the experiment. At 4 weeks of age, whole blood samples, obtained by cardiac puncture, from 5 males and 5 females per treatment, were heparinized, centrifuged and frozen for analyses. The same birds were sacrificed; livers and kidneys were removed and wrapped in foil and quick-frozen. Isocitric dehydrogenase activities of the plasma were determined by the method of Wolfson and Williams-Ashman (6). Succinic dehydrogenase and cytochrome oxidase activities of the livers and kidneys were determined by the methods of Cooperstein et al(7) and Cooperstein and Lazarow(8). Enzyme activities were measured with a Beckman Model B spectrophotometer and the data recorded on a coupled Bausch and Lomb V.O. M-5 strip chart recorder. Data obtained from these tests were subjected to an analysis of variance as outlined by Snedecor(9), and differences between treatment means were tested by the multiple range test of Duncan(l0).
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