Studies on the biosynthesis of heme from iron and protoporphyrin.
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منابع مشابه
Regulation of heme synthesis in erythroid cells: hemin inhibits transferrin iron utilization but not protoporphyrin synthesis.
The inhibition of delta-aminolevulinic acid (ALA) synthase activity by heme is commonly thought to regulate the overall rate of heme synthesis in erythroid cells. However, since heme inhibits erythroid cell uptake of iron from transferrin, we have tested the hypothesis that in reticulocytes heme regulates its own synthesis by controlling the cellular acquisition of iron from transferrin rather ...
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Nickel is an essential element for all living organisms such as microorganisms, plants and animals. When nickel concentration exceeds the necessary concentration, could be toxic, and likewise causes adverse effects in living organisms. In this study, following determining nickel LC50-96h for common carp (Cyprinus carpio), nickel sub-lethal treatments including 0 (control), 0.055, 0.275, 0.572, ...
متن کاملStudies on the biosynthesis of heme in vitro by avian erythrocytes.
I T IS now. knowim that glycimie’ and “active” succinate2 are precursors of protoporphyrin and heme amid that 5-anminolevulinic acid3’ and porphobilinogen68 are iimternmediates in this pathway. Although there has been some controversy9 as to whether free protoporphyrin itself is an iimtermediate in henme biosynthesis, recent work stroimgby supports this view.’#{176}’2 Thus, there is available f...
متن کاملEFFECT OF CHRONIC LEAD POISONING ON ERYTHROCYTE PROTOPORPHYRIN IN RATS
Research has shown that exposure to lead may have adverse effects at different blood lead concentrations. Lead inhibits at least two enzymes that are essential for the formation of heme, and because of the interaction of lead with these enzymes, no iron is inserted into protoporphyrin. Therefore the concentration of protoporphyrin increases in erythrocytes. The concentration of lead was mea...
متن کاملStudy of factors causing excess protoporphyrin accumulation in cultured skin fibroblasts from patients with protoporphyria.
The activity of heme synthetase, which catalyzes the chelation of ferrous iron to protoporphyrin to form heme, is deficient in sonicates of skin fibroblasts cultured from patients with protoporphyria. During culture in Eagle's medium supplemented with fetal calf serum, these cells do not accumulate protoporphyrin, however. This may be due to a minimal requirement for heme synthesis, since glyci...
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عنوان ژورنال:
- Blood
دوره 14 4 شماره
صفحات -
تاریخ انتشار 1959