Erythrocyte delta-aminolaevulinic acid dehydratase, urinary porphyrins and porphyrin precursors in iron deficiency anaemia. 1977

G Chalevelakis, and C Lyberatos, and D Manopoulos, and J Pyrovolakis, and C Gardikas

In 20 iron deficient patients and 21 normal controls the activity of the enzyme delta-ALA dehydratase of erythrocytes was assayed. In addition the urine porphyrins and porphyrin precursor excretions were measured. It was found that in sideropenic patients the erythrocyte delta-ALA dehydratase activity was almost constantly higher than in normals; the difference of the mean values being statistically significant (p less than 0.005). A significant diminution of delta-ALA (p less than 0.0025) urine excretion was observed, whereas the urine excretion of PBG, CP and UP was found within the normal limits. The results are compared to those reported by other authors.

UI MeSH Term Description Entries
D011166 Porphyrins A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin. Porphyrin
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006836 Hydro-Lyases Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1. Dehydratase,Dehydratases,Hydrase,Hydrases,Hydro Lyase,Hydro-Lyase,Hydro Lyases,Lyase, Hydro,Lyases, Hydro
D000623 Porphobilinogen Synthase An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24. Aminolevulinate Hydro-Lyase,Aminolevulinic Acid Dehydratase,ALA-Dehydrase,delta-Aminolevulinate Dehydratase,delta-Aminolevulinic Acid Dehydratase,ALA Dehydrase,Acid Dehydratase, Aminolevulinic,Acid Dehydratase, delta-Aminolevulinic,Aminolevulinate Hydro Lyase,Dehydratase, Aminolevulinic Acid,Dehydratase, delta-Aminolevulinate,Dehydratase, delta-Aminolevulinic Acid,Hydro-Lyase, Aminolevulinate,Synthase, Porphobilinogen,delta Aminolevulinate Dehydratase,delta Aminolevulinic Acid Dehydratase
D000747 Anemia, Hypochromic Anemia characterized by a decrease in the ratio of the weight of hemoglobin to the volume of the erythrocyte, i.e., the mean corpuscular hemoglobin concentration is less than normal. The individual cells contain less hemoglobin than they could have under optimal conditions. Hypochromic anemia may be caused by iron deficiency from a low iron intake, diminished iron absorption, or excessive iron loss. It can also be caused by infections or other diseases, therapeutic drugs, lead poisoning, and other conditions. (Stedman, 25th ed; from Miale, Laboratory Medicine: Hematology, 6th ed, p393) Chlorosis,Anemias, Hypochromic,Chloroses,Hypochromic Anemia,Hypochromic Anemias

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