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Protoporphyrinogen oxidase and ferrochelatase in porphyria variegata
Author(s) -
VILJOEN D. J.,
CUMMINS R.,
ALEXOPOULOS J.,
KRAMER S.
Publication year - 1983
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1983.tb00102.x
Subject(s) - protoporphyrinogen oxidase , ferrochelatase , porphyria , protoporphyrin ix , heme , chemistry , protoporphyrin , biochemistry , ascorbic acid , oxidase test , enzyme , endocrinology , porphyrin , medicine , food science , organic chemistry , photodynamic therapy
. Protoporphyrinogen oxidase activity and ferrochelatase activity were measured in leucocytes from patients with porphyria variegata. The mean activity of protoporphyrinogen oxidase (PPO) in porphyria variegata (PV) was about 50% of normal ( P < 0.05). The mean activity of ferrochelatase with 59 Fe 2+ sulphate and protoporphyrin as substrates (in the presence of ascorbic acid) was reduced by 40% ( P < 0.009). The mean activity of ferrochelatase with 59 Fe 3+ chloride and protoporphyrin as substrates (in the presence of reduced glutathione) was increased by 65% ( P < 0.005). Both are statistically highly significant. The findings are interpreted as follows: (a) The occurrence of a low level of protoporphyrinogen oxidase in PV is confirmed, (b) The findings indicate a concurrent structural change in ferrochelatase (this may be structurally related to (a) but no evidence of this is at present available).