The effects of acetate, metal cations, phenobarbitone, porphyrogens and substrates of glycine acyltransferase on the utilization of haem by rat liver apo-(tryptophan pyrrolase).
1. The utilization of haem by rat liver apo-(tryptophan pyrrolase) under basal conditions and after enhancement of the enzyme activity by various mechanisms was studied under the influence of treatments affecting various aspects of liver haem metabolism. 2. These treatments were: benzoate and p-aminobenzoate as substrates of glycine acyltransferase, acetate as an inhibitor of 5-aminolaevulinate synthase activity, enhancement of 5-aminolaevulinate dehydratase by aluminium, destruction of haem and inhibition of ferrochelatase by porphyrogens, increased haem utilization by phenobarbitone and enhancement of haem oxygenase activity by metal cations. 3. The results show that the haem saturation of the apoenzyme is sensitive to all these treatments. 4. The possible usefulness of tryptophan pyrrolase in studying the regulation of liver haem is suggested.
D000624:5-Aminolevulinate Synthetase / Q000037:antagonists & inhibitors; D000085:Acetates / Q000494:pharmacology; D000818:Animals; D001051:Apoenzymes / Q000378:metabolism; D001565:Benzoates / Q000494:pharmacology; D005294:Ferrochelatase / Q000037:antagonists & inhibitors; D006418:Heme / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D008670:Metals / Q000494:pharmacology; D010634:Phenobarbital / Q000494:pharmacology; D000623:Porphobilinogen Synthase / Q000378:metabolism; D011165:Porphyrinogens / Q000494:pharmacology; D051381:Rats; D013268:Stimulation, Chemical; D014366:Tryptophan Oxygenase / Q000378:metabolism*
D000085:Acetates; D001051:Apoenzymes; D001565:Benzoates; D008670:Metals; D011165:Porphyrinogens; D006418:Heme; D014366:Tryptophan Oxygenase; D000624:5-Aminolevulinate Synthetase; D000623:Porphobilinogen Synthase; D005294:Ferrochelatase; D010634:Phenobarbital