Hydroxylation of tryptophan by rat-liver extracts.
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To obtain a pure ornithine carbamoyltransferase for quality control in clinical chemistry, the authors compared human plasma and bovine liver ornithine carbamoyltransferase. The data show that the KM of both enzymes are similar (respectively 1.03 and 1.33 mmol when ornithine is used as substrate; 1.02 and 1.06 mmol with carbamyl phosphate). The following properties are shown to be equivalent: linearity of the enzymatic reaction, inhibition by higher substrate concentrations, and temperature denaturation. The similarities between the two enzymes indicate that bovine liver ornithine carbamoyltransferase can be used in clinical chemistry quality control.
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Marked inhibition of porphyrinogen carboxylyase was produced in vitro by cytosol fractions, deproteinized and free of porphyrins, obtained from livers of mice made porphyric by 9 weeks i.p. treatment with 25 micrograms/kg/week of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Inhibition was proportional to the amount of the fraction added, was increased by preincubation in the absence of the substrate and, once established, could not be reversed by dialysis. TCDD itself, added to the control enzyme in the incubation mixture, did not affect enzyme activity up to a concentration of 77 nM, which is 10 times higher than the liver TCDD concentration found after in vivo TCDD treatment.
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