Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
The present work tries to elucidate if the strong decrease of porphyrinogen carboxylase (PCL) observed in experimental porphyria caused by hexachlorobenzene (HCB) is due to the presence of an inhibitor or to a modification of the protein structure of the enzyme. For this purpose: a) cross-assays and...
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| Autores principales: | , , , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00016764_v34_n4_p393_RiosdeMolina |
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| Sumario: | The present work tries to elucidate if the strong decrease of porphyrinogen carboxylase (PCL) observed in experimental porphyria caused by hexachlorobenzene (HCB) is due to the presence of an inhibitor or to a modification of the protein structure of the enzyme. For this purpose: a) cross-assays and heating ones were performed in order to look for the existence of a compound, that present in porphyric animals, would be responsible for the decrease of PCL activity found in them; b) the effect in vitro of HCB, HCB metabolites and other related compounds was studied to find the inhibitor of PCL activity and to look for a structure-inhibitory effect relation, c) hepatic PCL from porphyric and normal rats was purified, and enzyme properties were comparatively studied looking for structural differences between the enzymes obtained from both animal lots. The results indicate that: a) the heat deproteinized porphyric liver preparation produces an inhibition on the normal preparation, but it is smaller than the decrease produced in vivo by the HCB on this enzyme activity; thus other reasons may explain this behavior of PCL in intoxicated animals: b) the HCB had no effect on PCL activity; the phenolic compounds exhibited inhibitions of variable extent that were increased by the presence of electrophilic substituents. |
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