An Iron-binding Component in Human Blood Plasma

Schade, Arthur L.; Caroline, Leona

doi:10.1126/science.104.2702.340

Cited by 317 publications

(45 citation statements)

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“…Iron is carried in the serum as a p globulin complex (SCHADE and CAROLINE, 1946). We have found close correlation between the total iron binding capacity and (3 globulin in healthy children and in the cases of kwashiorkor (Fig.…”

Section: Discussionmentioning

confidence: 69%

Serum Copper, Iron and Iron Binding Capacity in Kwashiorkor

Edozien¹,

Udeozo²

1960

Journal of Tropical Pediatrics

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Anaemia is a common, but not an invariable finding in kwashiorkor. (TROWELL, DAVIES and DEAN, 1954). Although the anaemia is not usually of the microcytic, hypochromic variety, iron therapy appears to be beneficial when given in combination with high protein diet (TROWELL and SIMPKISS, 1957). Until recently very little information was available about iron metabolism in kwashiorkor and the therapeutic use of iron has been empirical. In pigs, protein deficiency was found to cause a slight fall in plasma iron and a large fall in the total iron binding capacity (CARTWRIGHT and WINTROBE, 1948). LAHEY et al in a recent study of malnourished Mexican children reported a fall in serum copper, iron and iron binding capacity in kwashiorkor. (LAHEY et al 1958). In the present communication, we report the results of similar observations on malnourished Nigerian children. MATERIALS AND METHODSThe subjects include 150 new cases of kwashiorkor attending the Paediatric Clinic at University College Hospital, Ibadan, between March and December, 1958. They all showed the usual typical features of kwashiorkor namely oedema, growth retardation, muscle wasting and hypoproteinaemia and most of them had skin and hair changes. Protein estimations were done on all the patients, but serum copper, serum iron and iron binding capacity were determined in 30, 35 and 31 cases respectively.For normal controls blood was obtained over a period of months from four hundred children between 6 months and 5 years old by femoral vein puncture. Protein analyses were undertaken on all the samples, and serum copper, iron and iron binding capacity were estimated on 25, 37 and 37 children respectively. Blood was also collected from 400 adults and of these serum copper was estimated on 45 samples, serum iron on 48 samples and total iron binding capacity on 30 samples. This is part of a scheme to establish biochemical normals in Nigerians.The serum was separated by centrifugation and assayed on the same day, but when samples could not be processed on the day of collection they were stored in the refrigerator at 4°C, and analysed the next day.The method of MARRACK (1956) was used for assay of serum iron. For assay of iron binding capacity the serum was treated in the manner recommended by RAMSAY (1957) and the iron was determined by the method of MARRACK. Serum copper was determined by the diethyldithiocarbamate method of EDEN and GREEN after the copper was liberated with 6 N HC1 according to the technique recommended by VENTURA and KING (1951). It should be recorded here that we often found difficulty in precipitating the serum proteins in the kwashiorkor samples with 20 per cent trichloracetic acid but a clean supernatant was obtained by heating to boilin3 point. No difficulty was experienced with normal sera.Total serum protein was measured by the Biuret method of WOLFSON et al, (1948). The protein fractions were determined r.fter paper electrophoresis according to the procedure of FLYNN and DE MAYO (1951) by staining with azocarmine B and scanning with the "...

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Section: Discussionmentioning

confidence: 69%

Serum Copper, Iron and Iron Binding Capacity in Kwashiorkor

Edozien¹,

Udeozo²

1960

Journal of Tropical Pediatrics

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“…Conalbumin (which we now refer to as ovotransferrin) was purified in 1900 [50] and identified as the antimicrobial agent of raw egg white in 1946 [51]. Two years earlier it had been established that the antimicrobial properties of egg white were abolished by the addition of iron [52]. The iron binding protein of human serum, serotransferrin was purified by Schade and Caroline in 1946 [53] and its anti-bacterial properties, as well as their abolition by iron, established.…”

Section: Proteins Of Iron Transportmentioning

confidence: 99%

“…Two years earlier it had been established that the antimicrobial properties of egg white were abolished by the addition of iron [52]. The iron binding protein of human serum, serotransferrin was purified by Schade and Caroline in 1946 [53] and its anti-bacterial properties, as well as their abolition by iron, established. Working independently, Laurell and Ingelman [54] also purified the 'red' protein from pig plasma and in the same year Holmberg and Laurell [55] proposed the name 'transferrin', which has since replaced the name siderophilin originally utilised by the American workers.…”

Section: Proteins Of Iron Transportmentioning

confidence: 99%

Iron transport and storage

Crichton

Charloteaux-Wauters

1987

European Journal of Biochemistry

489

246

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“…Even though the first isolation of a member of the transferrin family, ovotransferrin, came in 1900 [29] it was not until 1944 that it a role was proposed for it [30]. Soon after, a similar protein, now known as serum transferrin, was isolated from blood plasma [31]. The transferrin family comprising four main members, each exhibiting a high affinity for iron (K d~ 10 -22 M ) [32], includes the serum transferrins, which transport iron from its site of absorption to the site of utilisation or storage, the lactoferrins, which possess antimicrobial properties, the ovotransferrins, a major component of egg white, and the melanotransferrins, found…”

Section: Transferrinsmentioning

confidence: 97%

Structure/Function Overview of Proteins Involved in Iron Storage and Transport

Sargent

Farnaud

Evans

2005

CMC

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Iron, the major trace element in the body, is an essential component of many proteins and enzymes. As low-molecular-weight iron is potentially toxic to cells, higher organisms express a number of proteins for the transport and storage of iron. We review our current understanding of the intestinal absorption of iron in the light of recently identified membrane proteins, namely the ferrric reductase, Dcytb, the two iron(II) transport proteins, DMT1 and ferroportin/Ireg1, and hephaestin, the membrane-bound homologue of the ferroxidase ceruloplasmin. Two types of mammalian transferrin receptor, TfR1 and TfR2, are now known to exist. The structure of TfR1 and its role in the process of receptor-mediated cellular uptake of iron are presented together with structural information on the iron storage protein ferritin. Mechanisms for the regulation of levels of TfR1 and ferritin, as well as other proteins involved in iron homeostasis, are discussed. Our current knowledge and understanding of the structure of members of the transferrin family of iron-binding proteins and the nature of the iron-binding centres in transferrins is presented, together with information on the processes of iron-uptake and iron-release by transferrin and a summary of the elements that have been found to bind to transferrins.

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An Iron-binding Component in Human Blood Plasma

Cited by 317 publications

References 3 publications

Serum Copper, Iron and Iron Binding Capacity in Kwashiorkor

Serum Copper, Iron and Iron Binding Capacity in Kwashiorkor

Iron transport and storage

Structure/Function Overview of Proteins Involved in Iron Storage and Transport

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