Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0240066 (iron deficiency)
 7,156 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Porphobilinogenase was isolated and purified from soya-bean callus tissue; its components, porphobilinogen deaminase and uroporphyrinogen isomerase, were separated and purified. 2. The purified porphobilinogenase was resolved into two bands on starch-gel electrophoresis. The molecular weights of porphobilinogenase, deaminase and isomerase fractions were determined by the gel-filtration method. Porphobilinogenase activity was affected by the presence of air; uroporphyrinogens were only formed under anaerobic conditions, although substrate consumption was the same in the absence of oxygen as in its presence. 3. pH-dependence of both porphobilinogenase and deaminase was the same and a sharp optimum at pH 7.2 was obtained. Isomerase was heat-labile, but the presence of ammonium ions or porphobilinogen afforded some protection against inactivation. The action of several compounds added to the system was studied. Cysteine, thioglycollate, ammonium ions and hydroxylamine inhibited porphobilinogenase; certain concentrations of sodium and magnesium salts enhanced activity; some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited the deaminase. 4. delta-Aminolaevulate and ethionine in the culture media stimulated porphyrin synthesis and increased porphobilinogenase activity, whereas iron deficiency resulted in porphyrin accumulation. 5. The development of chlorophyll and porphobilinogenase on illumination of dark-grown callus was followed. 6. A hypothetical scheme is suggested for the enzymic synthesis of uroporphyrinogens from porphobilinogen.
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PMID:Studies on the porphobilinogen deaminase-uroporphyrinogen cosynthetase system of cultured soya-bean cells. 516 54

Imferon (Merrell-National), an iron-dextran complex, is widely used in patients with iron deficiency. It is present in the circulation in appreciable amounts for two to three weeks after administration and interferes with all tested colorimetric iron assays, both with and without deproteinization. The amount of the plasma Imferon iron interference depends primarily on the choice of reductant. With dithionite it is essentially 100%. In the presence of ascorbic acid and hydroxylamine, the interference depends also on assay conditions, especially temperature, but also incubation time and pH. The minimum interference in a homogeneous assay was about 3%. The relative amount of interference from hemoglobin iron under the various assay conditions is different from that of Imferon iron. In the presence of a reducing agent, the dextran-iron complex decomposes--instantaneously with dithionite, and gradually with sulfite, ascorbic acid, and hydroxylamine. The freed iron becomes dialyzable, can react with bathophenanthroline, and elutes on a Sephadex G-50 or G-15 column in the same fractions as an ammonium ferrous sulfate.
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PMID:Interference of imferon in colorimetric assays for iron. 726 10