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At least 19 recordsLinked to original sources

PubMed1990

Colorimetry and constant-potential coulometry determinations of transferrin-bound iron, total iron-binding capacity, and total iron in serum containing iron-dextran, with use of sodium dithionite and alumina columns.

After the parenteral administration of iron-dextran (imferon), the increased total iron concentrations in serum can be determined by atomic absorption spectroscopy and by colorimetric methods involving sodium dithionite, which reductively dissociates iron from the dextran complex. We report that constant-potential coulometry detects only about 55-70% of dextran-bound iron before dithionite reduction and variable amounts after reaction with the reducing agent. In addition, we have developed a procedure for determining transferrin-bound iron, total iron-binding capacity (TIBC), total iron, and dextran-bound iron with the Kodak Ektachem colorimetric system. In determining total serum iron, the sample is first mixed with sodium dithionite, which rapidly dissociates all dextran-bound iron, but does not remove iron from either transferrin or hemoglobin. After the mixture is applied to an Ektachem slide, transferrin-bound iron is released at pH 4 and is detected together with the iron previously bound to dextran. TIBC is determined by mixing serum with ferric citrate in moderate excess and filtering through a small alumina (Al2O3) column, which binds excess free iron and iron-dextran; the iron in the column eluate represents the TIBC. Transferrin-bound iron is determined by applying diluted serum without added ferric citrate to an alumina column and measuring the iron in the column eluate. Dextran-bound iron is equivalent to the difference between total and transferrin-bound iron. Using this method, we found that transferrin iron-binding sites are saturated in vitro by excess iron-dextran less efficiently than by ferric citrate.

Aluminum Oxide↗

PubMed1990

Increased intestinal iron absorption in rats with normal hepatic iron stores. Kinetic aspects of the adaptative response to parenteral iron repletion in dietary iron deficiency.

Male Sprague-Dawley rats were fed an iron-deficient diet for 8 days. After this period, iron stores were repleted in three groups of animals by intravenous administration of iron dextran. In a second set of experiments, iron was administered in the same dose as Fe nitrilotriacetic acid complex. 12 h, 24 h and 48 h thereafter, the intestinal iron transfer in vitro and in vivo as well as the non-heme iron and ferritin content were determined in both the liver and the jejunal mucosa. In iron deficiency, intestinal iron transfer is increased to 230% of untreated controls, while non-heme iron and ferritin decreased to 20% and 10% in the liver and to 55% and 25% in the mucosa, respectively. 12 h and 24 h after parenteral administration of 0.1 mmol Fe/kg body weight iron transfer was as high as in iron deficiency, while liver iron stores were not significantly different from the untreated controls. In this situation, the close link between decreases in body iron stores and increases in iron transfer was temporarily dissociated. This can be related to the time lag between the incorporation of parenterally applied iron in the liver and in the jejunal mucosa. The data provide evidence for the hypothesis that the hepatic iron stores have no means of neural or hormonal communication with the small intestine in order to adapt iron transfer to their state of repletion on short notice. Intestinal iron transfer returned to control levels after 48 h.

Adaptation, Physiological↗

PubMed1976

[Comparison of the metabolism of 2 injectable iron preparations (sorbitol iron and polymaltose iron) with the metabolism of transferrin and hemoglobin iron].

Iron distribution in the different organs and chemical compartments of the rat has been studied after intravenous injection of 59Fe-sorbitol (Jectofer-Astra) and 59Fe-polymaltose (Fer Hausmann Lucien) and compared with the metabolism of 59Fe bound to transferrin and to hemoglobin. Both parenteral iron preparations are utilized more slowly than Iron-transferrin. The speed of red cell incorporation of 59Fe from sorbitol is similar to the hemoglobin iron utilization (half incorporation in red cells: 4 to 5 days). Iron polymaltose is much more slowly utilized (half incorporation in the red cells: 13 to 15 days). One third of the 59Fe from sorbitol is eliminated in urine, the remaining iron being taken up to 60% by the liver and to 30% by the bone marrow. It is very quickly catabolized, since as early as the first hour after injection most of the 59Fe is bound to polymaltose till the 14th day. Between the third and fourth week 25% of the 59Fe from polymaltose is found in hemosiderin. These metabolic differences are also found in man: 59Fe from iron sorbitol is found in urine after injection, is mobilized by desferrioxamine after six days, and eliminated through dialysis membranes. On the other hand the 59Fe from polymaltose is slowly but completely utilized and not mobilized by desferrioxamine in the first week after injection. The data give the indications for use and the pharmacokinetics of two forms of parenteral iron and oral preparations in the treatment of iron deficiency.

Animals↗

PubMed1989

[Women and iron deficiency--a problem? Iron levels in a group of fertile Norwegian women and the bioavailability of 3 low-dose iron supplements in women with low iron stores].

Serum ferritin levels were determined in 170 healthy Norwegian women (18-48 y, median age 36 y) including 23 blood donors. Exhausted iron stores, defined by serum ferritin levels less than 17 micrograms/l, were found in 21.8% of the non-donors, and in 30.4% of the donors. Women with serum ferritin levels less than or equal to 20 micrograms/l participated in a bioavailability study. They were randomized to one of three groups and given one of three different low dose iron supplements (18-20 mg iron per day) for six months. One of the supplements contained heme iron and non-heme iron, the other two contained non-heme iron only. Mean serum ferritin increase was significant for two of the supplements, the one containing heme iron giving the best result. All the supplements resulted in a significant decrease in TIBC.

Adult↗

PubMed1975

Bioavailability of trivalent iron in oral iron preparations. Therapeutic efficacy and iron absorption from simple ferric compounds and high- or low-molecular weight ferric hydroxide-carbohydrate complexes.

All available results from critical hemoglobin regeneration tests, postabsorption serum iron concentration studies, 59Fe erythrocyte incorporation and 59Fe whole-body retention measurements demonstrate that humans do absorb ferrous iron between 4 and 10 times (in the average about 5 times) better than ferric iron from therapeutic oral 50--250 mg iron doses. Ferrous sulfate iron is 3 to 4 times better available than the iron from ferric ammonium citrate or sulfate. Whereas 100 mg of ferrous sulfate iron/day are sufficient for an optimal oral compensation iron therapy and to produce initial hemoglobin regeneration rates of about 0.26 g/100 ml/day, 400 to 1000 mg of ferric iron/day are necessary for the same therapeutic effect because of the poor bioavailability of ferric iron. The ratio of the dose-absorption relationships for ferric and ferrous 59Fe was shown to decrease from 0.43 for a diagnostic 0.56 mg Fe dose to 0.21 for the therapeutic 50 mg Fe dose in subjects with normal iron stores. Absorption ratios of 0.65 for the 0.56 mg Fe dose and 0.26 for the 50 mg Fe dose were measured in subjects with depleted iron stores. At all dose levels the superior bioavailability of ferrous iron was demonstrable. A high-molecular weight ferric hydroxide-carbohydrate complex (MW similar to 30 000) was palatable but so poorly absorbed that is was practically without effect on hemoglobin regeneration even at a daily 300 mg Fe dose. Following several warnings such a useless commerecial oral iron preparation was finally withdrawn from the market. The iron from any high-molecular weight carbohydrate complex of ferric hydroxide has to be suspected to be poorly absorbed and therefore therapeutical useless, unless the opposite has been demonstrated with a reliable bioassay (59Fe absorption whole-body retention and hemoglobin regeneration test). A low-molecular weight so-called ferric hydroxide-fructose complex was shown to contain iron of more or less the same poor bioavailability as contained in ferric chloride since the iron from ferrous sulfate was about 5 times better absorable. The good absorption of ferrous sulfate iron was not further augmented by even very large oral doses of fructose since this carbohydrate did not improve the ferrous iron absorption at a fructose: Fe molar ratio of 106:1. Trivalent iron in simple compounds like ferric ammonium citrate or in low- and high-molecular weight carbohydrate complexes of ferric hydroxide is so poorly available for intestinal iron absorption in man that it cannot be used for a fast and reliable oral iron therapy with reasonably low doses as it can be easily practised with quick-lease preparations of ferrous sulfate at a 100 mg Fe2

Anemia, Hypochromic↗

PubMed1992

Deferoxamine-induced iron mobilization and redistribution of myocardial iron in cultured rat heart cells: studies of the chelatable iron pool by electron microscopy and Mössbauer spectroscopy.

Iron mobilization by deferoxamine from iron-loaded rat heart cells in culture was studied by electron microscopy and Mössbauer spectroscopy to identify the chelatable iron pool. Studies in which iron 59 was used have shown a diminishing response to deferoxamine with increasing time intervals, which suggests a gradual transit from a more available to a less available storage iron compartment. Mössbauer spectroscopy showed that practically all iron mobilized by deferoxamine was derived from the small (less than 3.0 nm) recently acquired iron particles, which supports the "last-in, first-out" principle. Quantitation of cytosolic ferritin iron particles has shown a highly reproducible increase in cytosolic ferritin iron after deferoxamine treatment. This intracellular redistribution of iron stores is explained either by a reduced transfer of cytosolic ferritin into siderosomes or, more likely, by increased mobilization of membrane-bound iron deposits from insoluble polynuclear iron complexes in siderosomes and their subsequent incorporation into cytosolic ferritin. Thus the protective effect of deferoxamine on iron-loaded heart cells may be twofold: (1) net removal of excess iron by the formation of a stable complex of iron with deferoxamine and its secretion into the extracellular environment and (2) a shift of solubilized iron from membrane-bound deposits into the cytosol where iron is detoxified by its incorporation into the hollow shell of the ferritin protein.

Animals↗

PubMed1991

Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. III. Import, protease processing, and assembly into the cytochrome bc1 complex of iron-sulfur protein lacking the iron-sulfur cluster.

We have used site-directed mutagenesis of the Saccharomyces cerevisiae Rieske iron-sulfur protein gene (RIP 1) to convert cysteines 159, 164, 178, and 180 to serines, and to convert histidines 161 and 181 to arginines. These 4 cysteines and 2 histidines are conserved in all Rieske proteins sequenced to date, and 4 of these 6 residues are thought to ligate the iron-sulfur cluster to the apoprotein. We have also converted histidine 184 to arginine. This histidine is conserved only in respiring organisms. The site-directed mutations of the six fully conserved putative iron-sulfur cluster ligands result in an inactive iron-sulfur protein, lacking iron-sulfur cluster, and failure of the yeast to grow on nonfermentable carbon sources. In contrast, when histidine 184 is replaced by arginine, the iron-sulfur cluster is assembled properly and the yeast grow on nonfermentable carbon sources. The site-directed mutations of the 6 fully conserved residues do not prevent post-translational import of iron-sulfur protein precursor into mitochondria, nor do the mutations prevent processing of iron-sulfur protein precursor to mature size protein by mitochondrial proteases. Optical spectra of mitochondria from the six mutants indicate that cytochrome b is normal, in contrast to the deranged spectrum of cytochrome b which results when the iron-sulfur protein gene is deleted. In addition, mature size iron-sulfur apoprotein is associated with cytochrome bc1 complex purified from a site-directed mutant in which iron-sulfur cluster is not inserted. These results indicate that mature size iron-sulfur apoprotein, lacking iron-sulfur cluster, is inserted into the cytochrome bc1 complex, where it interacts with and preserves the optical properties of cytochrome b. Insertion of the iron-sulfur cluster is not an obligatory prerequisite to processing of the protein to its final size. Either the processing protease cannot distinguish between iron-sulfur protein with or without the iron-sulfur cluster, or insertion of the iron-sulfur cluster occurs after the protein is processed to its mature size, possibly after it is assembled in the cytochrome bc1 complex.

Amino Acid Sequence↗

PubMed1992

Salivary iron status in children with iron deficiency and iron overload.

Forty anaemic (iron deficiency anaemia-27, thalassemia major-8, and aplastic anaemia-5) and 10 non-anaemic children (serving as controls) aged from 8 months to 10 years were selected for the study. The salivary iron was significantly higher in iron deficient and iron overload conditions compared to controls. The mean salivary:serum iron ratio was same in control and iron overload cases, while it was twice as high in iron deficient anaemic children. The correlation between salivary iron and serum iron was significant (r = 0.7392, P less than 0.001) in these cases. The iron deficient anaemic children with hypoalbuminaemia had significantly reduced serum and salivary protein (P less than 0.001), but iron concentrations in serum and saliva remained unaltered. The salivary protein level had significant correlations with serum albumin and serum protein (P less than 0.001). Thus, the iron in saliva is maintained at a higher level and more so in iron deficiency anaemia; it correlates well with serum iron (r = 0.6853, P less than 0.001) in iron deficient anaemic children also and is not affected by co-existing hypoproteinaemic situation.

Albumins↗

PubMed1989

Biochemistry of nonheme iron in man. I. Iron proteins and cellular iron metabolism.

Total plasma iron turnover in man is about 36 mg/day. Transferrin is the iron transport protein of plasma, which can bind 2 atoms of iron per protein molecule, and which interacts with various cell types to provide them with the iron required for their metabolic and proliferative processes. All tissues contain transferrin receptors on their plasma membrane surfaces, which interact preferentially with diferric transferrin. In erythroid cells as well as certain laboratory cell lines, the removal of iron from transferrin apparently proceeds via the receptor-mediated endocytosis process. Transferrin and its receptor are recycled to the cell surface, whereas the iron remains in the cell. The mode of iron uptake in the hepatocyte, the main iron storage tissue, is less certain. The release of iron by hepatocytes, as well as by the reticuloendothelial cells, apparently proceeds nonspecifically. All tissues contain the iron storage protein ferritin, which stores iron in the ferric state, though iron must be in the ferrous state to enter and exit the ferritin molecule. Cellular cytosol also contains a small-molecular-weight ferrous iron pool, which may interact with protoporphyrin to form heme, and which apparently is the form of iron exported by hepatocytes and macrophages. In plasma, the ferrous iron is converted into the ferric form via the action of ceruloplasmin.

Animals↗

PubMed1991

Lactoferrin inhibits or promotes Legionella pneumophila intracellular multiplication in nonactivated and interferon gamma-activated human monocytes depending upon its degree of iron saturation. Iron-lactoferrin and nonphysiologic iron chelates reverse monocyte activation against Legionella pneumophila.

We have been exploring the role of iron in the pathogenesis of the intracellular bacterial pathogen Legionella pneumophila. In previous studies, we have demonstrated that L. pneumophila intracellular multiplication in human monocytes is iron dependent and that IFN gamma-activated monocytes inhibit L. pneumophila intracellular multiplication by limiting the availability of iron. In this study, we have investigated the effect on L. pneumophila intracellular multiplication of lactoferrin, an iron-binding protein which is internalized via specific receptors on monocytes, and of nonphysiologic iron chelates which enter monocytes by a receptor-independent route. Apolactoferrin completely inhibited L. pneumophila multiplication in nonactivated monocytes, and enhanced the capacity of IFN gamma-activated monocytes to inhibit L. pneumophila intracellular multiplication. In contrast, iron-saturated lactoferrin had no effect on the already rapid rate of L. pneumophila multiplication in nonactivated monocytes. Moreover, it reversed the capacity of activated monocytes to inhibit L. pneumophila intracellular multiplication, demonstrating that L. pneumophila can utilize iron from the lactoferrin-lactoferrin receptor pathway. The capacity of iron-lactoferrin to reverse monocyte activation was dependent upon its percent iron saturation and not just its total iron content. Similarly, the nonphysiologic iron chelates ferric nitrilotriacetate and ferric ammonium citrate completely reverse and ferric pyrophosphate partially reversed the capacity of IFN gamma-activated monocytes to inhibit L. pneumophila intracellular multiplication, demonstrating that L. pneumophila can utilize iron derived from nonphysiologic iron chelates internalized by monocytes independently of the transferrin and lactoferrin endocytic pathways. This study suggests that at sites of inflammation, lactoferrin may inhibit or promote L. pneumophila intracellular multiplication in mononuclear phagocytes depending upon its degree of iron saturation. In addition, this study suggests a potential role for PMN in host defense against L. pneumophila--providing apolactoferrin to infected monocytes--and it supports the concept that PMN and monocytes may cooperate in host defense against intracellular parasites and other pathogens.

Apoproteins↗

PubMed1990

Response of various indices of iron status to acute iron depletion produced in menstruating women by low iron intake and phlebotomy.

We investigated response sensitivities of indices of iron status to controlled iron depletion and repletion in 11 premenopausal women. The women were depleted of storage iron (as reflected by serum ferritin) through a combination of a low-iron diet and phlebotomy. They then consumed a diet containing 13.7 mg of iron per 2000 kcal, supplemented with either ascorbic acid or placebo (for 5 1/2 weeks) and a daily 50-mg iron supplement (for the subsequent 17 days). The relative sensitivities of different indices for detecting iron depletion were as follows: ferritin greater than % transferrin saturation greater than plasma iron greater than hemoglobin greater than hematocrit greater than zinc protoporphyrin (ZnPP) and erythrocyte protoporphyrin (EP). Ascorbic acid treatment during repletion, before iron supplementation, significantly (P less than 0.05) affected changes in hemoglobin, ZnPP, ZnPP/heme, and EP/heme. Changes in heme synthesis evidently do not occur until iron stores are depleted and, conversely, during iron repletion hematopoiesis must be satisfied before iron stores, as reflected by ferritin, increase. Thus, the use of only one index of iron status is of limited value for detecting iron depletion.

Adult↗

PubMed1992

Regulation of iron absorption in iron loaded subjects with end stage renal disease: effects of treatment with recombinant human erythropoietin and reduction of iron stores.

The effects on iron absorption of variation in erythroid activity, haemoglobin and iron stores were studied in six anaemic dialysis-dependent subjects in whom iron stores were increased from previous red cell transfusions. Gastrointestinal mucosal uptake and whole body retention of oral iron were measured at the beginning of the study, after starting treatment with recombinant erythropoietin (but before significant increase in haemoglobin), after partial correction of anaemia, after further reduction of iron stores by repeated phlebotomy, and when erythropoiesis decreased from the discontinuation of treatment with erythropoietin. Between successive measurements, valid comparisons were made in five subjects. Correction of anaemia decreased whole body retention of iron through decreased mucosal uptake (P = 0.032). Further reduction in iron stores through repeated phlebotomy whilst the increase in haemoglobin was maintained by treatment with erythropoietin, tended to increase whole body retention of iron through an increase in mucosal transfer (P = 0.010). With initial enhancement of erythropoiesis in anaemic iron-loaded subjects there was no change in any measured component of iron absorption. However, after correction of anaemia and reduction of iron stores, a decrease in erythropoiesis was associated with decreased whole body iron retention in all subjects through decreased mucosal transfer (P = 0.028). The data suggest that anaemia upregulates mucosal iron uptake, and that erythroid activity upregulates mucosal transfer but that this latter effect may be counter-balanced by iron overload which downregulates mucosal transfer.

Adult↗

PubMed1979

Iron and the liver: subcellular distribution of iron and decreased microsomal cytochrome P-450 in livers of iron-loaded rats.

To understand better the intracellular iron distribution and metabolic consequences of chronic hepatic iron overload, rats were given large doses of iron dextran or ferric citrate intraperitoneally. They accumulated large quantities of iron within Kupffer cells and hepatocytes. The relative subcellular iron distributions were similar in controls and iron-loaded rats, despite a ten- to 20-fold difference in hepatic iron concentration. Electron microscopy of whole liver and subcellular particulate fractions suggested that iron was present in highest concentration in lysosomes, which were rendered more labile by its presence. Nevertheless, quantitative iron determinations on all subcellular fractions, obtained by two preparative methods, showed that most of the iron was present in the "soluble" fraction. The amount of iron in the "microsomal" fraction varied, depending on the techniques used for preparation of this fraction. Cytochrome P-450 and total heme concentrations were decreased 40% to 50% in microsomes isolated from iron-loaded livers.

Animals↗

PubMed1989

Studies of iron:zinc interactions in adult rats and the effect of iron fortification of two commercial infant weaning products on iron and zinc status of weanling rats.

The effect of iron on zinc absorption in the rat, and vice versa, was investigated from single starch:sucrose test meals (containing 65Zn or 59Fe) by whole body counting. Zinc had no effect on iron absorption, but iron reduced zinc absorption when the total ionic species in the meal (iron plus zinc) reached 1.36 mg. Below this level, high iron:zinc molar ratios (10:1) had no effect on zinc absorption, presumably because the transport mechanism for zinc had not reached full capacity. Previous iron intake had no effect on zinc absorption. The relevance of these findings to infant foods was explored by feeding rats exclusively a vegetable or cereal weaning product, with or without additional iron, for 12 d and measuring zinc and iron status. The added iron raised body iron stores and caused a small reduction in zinc status in animals fed the oat, but not the vegetable, diet as measured by plasma and femur zinc concentrations. Since the threshold level of 1.36 mg ionic species would be exceeded when the animal ate 3-4 g of the iron-fortified weaning food at any one time, it appears that the iron:zinc interactive effect was absent in the vegetable and less potent in the oat formulation than in a carbohydrate test meal. Alternatively, it may be the case that the animals had responded over time to reduced zinc availability by increasing whole body zinc retention.(ABSTRACT TRUNCATED AT 250 WORDS)

Absorption↗

PubMedDate not supplied

Anemia associated with changes in iron and iron-59 utilization in copper deficient rats fed high levels of dietary ascorbic acid and iron.

The influence of dietary copper, iron, and ascorbic acid on iron utilization was examined in a 2 x 2 x 2 factorial experiment. Male Sprague-Dawley weanling rats were fed copper-deficient (Cu-, 0.42 microgram Cu/g) or copper-adequate (Cu+, 5.74 micrograms Cu/g) diets that contained one of two levels of iron (38 or 191 micrograms Fe/g) and ascorbic acid (0 or 1% of the diet). These eight diets were fed for 20 d, and rats received an oral dose of 4 microCi iron-59 on d 15. Compared to Cu+ rats, the Cu- rats had 27% lower hemoglobin levels with 45, 59, and 65% lower cytochrome c oxidase (CCO) activities in the liver, heart, and bone marrow, respectively (p less than 0.0001). High dietary iron or ascorbic acid did not alter hemoglobin in Cu+ rats. However, hemoglobin was 23% lower in Cu- rats fed the highest, rather than the lowest levels of iron and ascorbic acid. Liver CCO was decreased (p less than 0.02) in Cu- rats fed high iron. Among Cu- rats, ascorbic acid did not influence CCO but decreased hemoglobin by 17% (p less than 0.001), reduced the percentage of absorbed iron-59 in the erythrocytes by 91% (p less than 0.05) and depressed the percentage apparent absorption of iron (p less than 0.05). These results suggest that the effects of elevated dietary iron and ascorbic acid on iron utilization are influenced by copper status.

Anemia, Hypochromic↗

PubMed1992

Iron absorption from chewable vitamins with iron versus iron tablets: implications for toxicity.

The medical literature contains few, if any, reports of severe iron (Fe) poisonings from ingestion of chewable multivitamins with iron. One possible explanation for this observation is that iron from multivitamins is more poorly absorbed than iron from iron tablets. To compare iron absorption from multivitamins with iron absorption from ferrous fumarate tablets, male adult volunteers were given 6 mg of elemental Fe/kg body weight as chewable multivitamins with iron or as crushed ferrous fumarate tablets in a crossover study. Serum Fe and total iron binding capacity (TIBC) were determined prior to administration of the tablets and one, two, four, and six hours after ingestion. Statistical analyses demonstrated increased and more rapid absorption of Fe from the multivitamin preparation. These results suggest that iron is well absorbed from chewable multivitamins with iron and should theoretically have the potential for producing serious toxicity when taken in overdose. The reasons that such toxicity is not commonly seen clinically are discussed, and a plan for further investigation of this issue is proposed.

Adult↗

PubMed1975

Iron absorption in early pregnancy - a study of the absorption of non-haeme iron and ferrous iron in early pregnancy.

The absorption of non-haeme iron in the food and from a 3 mg reference dose of ferrous iron in solution was measured in 17 healthy women before the 12th week of gestation and in 13 of the women two months after legal abortion. The absorption of ferrous iron in solution was calculated from determinations of the 55Fe activity in blood samples. The food iron absorption was measured from 59Fe-labelled test meals using a highly sensitive whole-body counter. In addition bone-marrow smears and other haematological parameters were studied. The median value of the absorption from the non-haeme food iron was 2.5% and from the ferrous iron salt 10.0 % in early pregnancy in women with storage iron. Two months after abortion the absorption increased to 12.6 and 42.6 % respectively. In early pregnancy the absorption of iron was higher in women without stainable iron in bone-marrow smears. The present results confirm previous observations that the absorption of food iron in early pregnancy is lower than the basal daily requirements. The low absorption is only partly explained by the reduced requirements of iron in early pregnancy. Some other factors related to pregnancy seem also to be involved.

Abortion, Induced↗

PubMed1991

[Iron stores, iron deficiency and iron supplementation].

In order to assess the prevalence of iron deficiency in the Danish population, a randomised cross sectional investigation was carried out one year after repealing of the order from 1939 concerning supplementing of corn products with iron. A randomised group of 198 persons divided into ten groups of 20 persons with equal numbers of men and women in the age group 20-69 years was submitted to determinations of serum-iron, serum-transferrin and serum-ferritin. The prevalence of iron deficiency as determined by serum-ferritin values of below 15 micrograms/l was 18% and 12% respectively, for women under and over 45 years while iron deficiency determined by transferrin saturation under 16% was 18% for both groups. 6% of the women under 45 years had severe iron deficiency as determined by low transferrin saturation and low ferritin. The prevalence among men was 1% and 3% as assessed by serum-ferritin levels and transferritin saturation. These results were compared with corresponding population investigations from Sweden where iron enrichment is the highest in the world and the sale of iron tablets is the greatest in the world. No significant differences in the frequency of latent iron deficiency could be demonstrated but the number of persons with severe iron depletion appears to be less in Sweden. Differences in the methodological procedures, however, cannot be excluded.

Adult↗