Protoporphyrinogen oxidase and porphobilinogen deaminase in variegate porphyria.
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| Abstract |
Two enzymes of the haem biosynthetic pathway were investigated in patients with variegate porphyria. Protoporphyrinogen oxidase in cultures of Epstein-Barr virus transformed lymphoblasts from twenty-seven patients showed a mean maximal velocity (Vmax) of 0.39 +/- 0.08+ nmol of protoporphyrin mg protein-1 h-1, a 52% reduction (P less than 0.001) from a non-porphyric control group (0.82 +/- 0.10). Km values (1.00 +/- 0.27 microM) did not differ significantly (P greater than 0.05) from control values in any of the patients. The mean Vmax of porphobilinogen deaminase in the cultures was 1.50 +/- 0.18 nmol of uroporphyrin mg protein-1 min-1, a 24% reduction (P less than 0.001) from controls (1.94 +/- 0.14). Mean porphobilinogen deaminase activity in the erythrocytes of twenty-one patients with variegate porphyria was 8.37 +/- 1.99 nmol of uroporphyrin 1 erythrocytes-1 s-1, a 28% reduction (P less than 0.001) from normal (11.98 +/- 2.11). The reduced activities of these two enzymes comply with the expression of variegate porphyria during its quiescent and acute phases.
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| Authors | P N Meissner, R S Day, M R Moore, P B Disler, E Harley |
| Journal | European journal of clinical investigation (Eur J Clin Invest) Vol. 16 Issue 3 Pg. 257-61 (Jun 1986) ISSN: 0014-2972 [Print] England |
| PMID | 3015635 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
| Chemical References |
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