Erythropoietic protoporphyria: Evidence that it is due to a variant ferrochelatase
International Journal of Biochemistry, ISSN: 0020-711X, Vol: 12, Issue: 5, Page: 925-930
1980
- 6Citations
- 5Captures
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Metrics Details
- Citations6
- Citation Indexes6
- CrossRef6
- Captures5
- Readers5
Article Description
Erythroid ferrochelatase activity was measured at different pH and temperature values in normal subjects and patients with porphyria variegate (PV) and erythropoietic protoporphyria (EPP). The pH activity curves were similar but whereas in PV patients and normal subjects the plots of ferrochelatase activity vs temperature were monophasic in EPP they were truncated. In addition zinc did not form a zinc protoporphyrin complex in fibroblasts from cases of EPP. These findings support the concept that erythropoietic protoporphyria is due to a genetic mutation resulting in a variant ferrochelatase.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0020711X8090186X; http://dx.doi.org/10.1016/0020-711x(80)90186-x; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0019247957&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/7450150; https://linkinghub.elsevier.com/retrieve/pii/0020711X8090186X; http://linkinghub.elsevier.com/retrieve/pii/0020711X8090186X; http://api.elsevier.com/content/article/PII:0020711X8090186X?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:0020711X8090186X?httpAccept=text/plain; http://dx.doi.org/10.1016/0020-711x%2880%2990186-x; https://dx.doi.org/10.1016/0020-711x%2880%2990186-x
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