Breath acetone is a reliable indicator of ketosis in adults consuming ketogenic meals

https://hal.archives-ouvertes.fr/hal-01186806/document

Metabolic and production profiles of dairy cows in response to decreased nutrient density to increase physiological imbalance at different stages of lactation

• The purposes of this study were to characterize the temporal relationship of distant organ dysfunction after mesenteric ischemia/reperfusion (l/R), and to ascertain if the neutrophil is critical to this process. Normal and neutrophildepleted rats (vinblastine sulfate, 0.75 mg/kg intravenously) underwent 45 minutes of superior mesenteric artery occlusion and after 0, 6, and 18 hours of reperfusion, blood was sampled and liver and lungs were harvested. Iodine 125 albumin leak was used as a marker for pulmonary and liver injury, and serum acetoacetate/3-hydroxybutyrate (AcAc/3-OHB) was used as an index of hepatic mitochondrial redox state. Gut l/R at 6 hours increased125l-albumin lung/blood ratio (gut l/R, 0.077±0.006; control, 0.045±0.004) and125l-albumin liver/blood ratio (gut l/R, 0.120±0.007; control, 0.077±0.003), while AcAc/3-OHB decreased significantly (gut l/R, 0.420±0.040; control, 0.880±0.120). Neutrophil depletion eliminated these changes at 6 hours (blood AcAc/3-OHB, 0.720±0.100;125l liver/blood, 0.068±0.006;125lung/blood, 0.046±0.007). We conclude the following: (1) intestinal l/R produces simultaneous liver and lung injury; (2) injury was present at 6 hours but is reversed at 18 hours; and (3) the l/R-induced liver and lung injuries were neutrophil mediated. (Arch Surg. 1992;127:175-179)

Liver injury is a reversible neutrophil-mediated event following gut ischemia.

Breath acetone predicts plasma ketone bodies in children with epilepsy on a ketogenic diet

The use in amperometric enzyme assays of a highly stable, pH insensitive flavoenzyme, reduced nicotinamide adenine dinucleotide oxidase (NADH oxidase), from the thermophilic organism Thermus aquaticus is described. The enzyme catalyses the oxidation of reduced nicotinamide adenine dinucleotide with concomitant two-electron reduction of dioxygen to hydrogen peroxide. In addition the enzyme used a substituted ferrocene as an alternative mediator of electron transfer. Hydrogen peroxide was detected at +650 mV vs Ag/AgCl at a platinum electrode. The current produced by oxidation of hydrogen peroxide was directly proportional to NADH concentration. The enzyme was used in solution to reoxidize enzymatically generated NADH and served as a basis for amperometric enzyme amplification systems for immunoassay as well as for the detection of substrate concentration for oxidoreductase enzymes. In the presence of alcohol dehydrogenase a rapid production of current occurred upon addition of ethanol over a clinically significant range. Thermus aquaticus NADH oxidase appears to be ideally suited for future exploitation in amperometric sensors for oxidoreductase substrates, offering a number of advantages over previously reported methods.

Thermostable reduced nicotinamide adenine dinucleotide oxidase: application to amperometric enzyme assay.

Direct automated assay method for serum or urine levels of ketone bodies.

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Direct automated assay method for serum or urine levels of ketone bodies.