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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The course of zinc protoporphyrin research has progressed at an increasingly rapid pace on several fronts. A variety of biochemical and clinical evidence viewed in toto now suggests that ferrochelatase catalyzes zinc protoporphyrin formation in states of relative iron-deficient erythropoiesis and in lead-inhibited iron metabolism. Furthermore, a redefinition of the relationship of zinc protoporphyrin to certain other parameters of iron status has been made based upon changes during the earliest states of iron depletion. These clinical studies show that the zinc protoporphyrin level and the ferritin level vary in concert but that changes in the percent transferrin saturation and in the hematocrit results are less consistent. Thus zinc protoporphyrin and ferritin are closely linked metabolically such that iron-deficient erythropoiesis becomes an initial manifestation of iron depletion. The measurement and expression of results as mumoles zinc protoporphyrin/mole heme have improved the quality of results, partly by the elimination of the assumed hematocrit designed into existing instruments. Other refinements in hematofluorometry technology have permitted exploration of the potentially extensive applications of zinc protoporphyrin measurements for lead surveillance and diagnosis, blood banking, pediatrics, obstetrics, sports medicine, and other clinical situations where a very sensitive, cost-effective indication of iron status is required.
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PMID:Zinc protoporphyrin. Past, present, and future. 332 39

Ferrochelatase with an Mr of 42,700 Da and a pI of 7.35 has been purified to homogeneity from chironomidae larvae. The activity of the enzyme reached maximum at pH 7.8 and decreased with the increase of pH. The enzyme activity varied with temperature and showed maximum activity around 37 degrees C. The purified enzyme was active towards protoporphyrin but inactive towards other porphyrins. The specific enzyme activity of ferrochelatase from chironomidae is about 10-fold higher than that of the rat. Electrophoresis of the purified fractions shows that the enzyme contains only one single polypeptide. The soluble ferrochelatase contained one mole of iron in each mole of the enzyme. The N-terminal sequence analysis of the enzyme shows a high percentage of conserved regions of the enzyme among other species. The enzyme properties are similar to those of the mammalian ferrochelatases except with slightly higher specific activity. Chironomidae ferrochelatase appeared to be more heat resistant and less susceptible than its mammalian equivalent to inhibition by lead.
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PMID:Purification and properties of ferrochelatase from Chironomidae larvae. 1145 77