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Different characteristics of ferrochelatase in cultured fibroblasts of erythropoietic protoporphyria patients and normal controls
Ist Teil von
Biochimica et biophysica acta, 1990-07, Vol.1039 (3), p.339-342
Ort / Verlag
Netherlands: Elsevier B.V
Erscheinungsjahr
1990
Quelle
Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
Beschreibungen/Notizen
Ferrochelatase activity was measured in crude extracts of fibroblasts, obtained from erythropoietic protoporphyria patients and healthy controls. The enzyme activity in erythropoietic protoporphyria fibroblasts was about 50% lower, compared to the controls. The sulfhydryl-oxiding reagent diamide inhibited the normal enzyme by about 50%, whereas ferrochelatase from erythropoietic protoporphyria fibroblasts was completely insensitive to the reagent.
Pb
2+
inhibits ferrochelatase activity by reacting with essential sulfhydryl groups. Low concentrations of
Pb
2+
inhibited the normal enzyme by 56%, but the mutant enzyme by only 8%. The photodynamic activity of bound mesoporphyrin substrate caused a biphasic inactivation of the normal enzyme.During the first 5 min of illumination a fast decrease of enzyme activity occured to about 60% of the initial value. Experimental evidence indicates that this first phase of inactivation is caused by photooxidation of sulfhydryl groups. Durings further illumination inactivation continued at a much slower rate. With ferrochelatase from erythropoitic protoporphyria fibroblasts only the second, slow phase of photodynamic inactivation was observed. These observations suggest a mutation of ferrochelatase in erythropoietic proporphyria, affecting the reactivity of sulfhydryl groups, involved in the catalytic of activity of the enzyme.