TOTAL CAPACITY OF IRON FIXATION
SYNONYMS: • iron binding capacity, CFTH,, CFH, TIBC, human transferrin test NORM
AL VALUES: Adult Aged Child. Newborn to 2 years 4 months Mayor TRANSFERRIN • • •
Adult: 200-400 mg / 100 ml Newborns: 130-275 mg / 100 ml Children: 203-360 mg /
100 ml 250-450 ¶ g/100 ml and adults 60 ¶ g/100 ml -175 100-400 350-400 ¶ g/100
ml ¶ g/100 ml
Iron is needed to produce hemoglobin, the iron is stored in different components . Transferrin, also called siderofilina is a beta globulin carrier protein that regulates the absorption of iron. The abundance of transferrin is related to the ability of the body to attack certain infections. The iron-binding capacity is correlated with serum transferrin, but this relationship is not linear. A test o f serum iron and transferrin without CFTH has very limited value with exceptions in cases of iron poisoning. Transferrin saturation is a better index of iron sa turation values as follows. Saturation = serum iron x 100 / CFTH Iron enters the body in the ferrous state. Once absorbed it transports a protein called the iro n. It combined the iron combines its ferric state. The ability to combine with i ron transferrin is measured as iron-binding capacity and its concentration has a constable consistency. Usually, but not always, conditions that lower concentra tions of serum iron increases the total fixation, ie, the more iron available to bind, the greater the number of total binding sites, that is, the more iron ava ilable to bind, the greater the number of empty binding sites. The ability to se t transferrin iron is about three times the normal serum iron. Usually the perce ntage saturation of TFH is calculated when the latter practice. This percentage represents the ratio of serum iron with the concentration CTHF. It follows a diu rnal pattern to a large extent, similar to serum iron, with its highest value du ring the morning and the lowest, in the late afternoon and start the evening. Va lues below 15% indicate a deficiency of iron deficiency anemia or iron-deficient erythropoiesis.
CLINICAL UTILITY • The combination of transferrin, iron and CFTH is very useful in the differential diagnosis of anemia in the assessment of iron deficiency ane mia and thalassemia, and sideroblastic anemias of hemochromatosis. CLINICAL SIGN IFICANCE transferrin increases in: • iron deficiency anemia. • Pregnancy. • estr ogen therapy. • Contraceptives. Transferrin decreases in • macrocytic anemia of chronic disease. • protein deficiency or loss of burns. • Chronic infection. • M alnutrition. • Kidney. • genetic deficiency. The iron-binding capacity increases in: • iron deficiency. • Use of contraceptives. • Pregnancy. • Chronic and acut e hemorrhage. • Acute hepatitis. The iron-binding capacity decreases in • Hypopr oteinemia (malnutrition and burns). • Hemochromatosis. • Anemia (infection and c hronic diseases). • Cirrhosis of the liver. • nephrosis and other renal disease. • Anemias indefinite non-iron. PREPRACION PATIENT: No s e required.
Ferritin serum iron
Introduction ferritin, ferric hodroxido complex and a protein, apoferririna, ori
ginates in the system reticuloendoelial. Ferritin reflects iron stores and is a
good indicator on the study of these stores. METHODS • SAMPLE • Serum Assay (ELI
SA) test fluoroenzimunometrico, colorimetric, inmunoenzimometrico, radiometrito.
STORAGE • Room temperature: 8 hours Refrigerated: 2 days, Frozen: 3 months. CON
TRAINDICATIONS • Sera severely hemolysates not repeatedly freeze and thaw the sa
mples. Strongly mixing may denature ferritin. NORMAL VALUES AGE 0-6 months 7-36
months 3-14 years 20-29 years 15-19 years 30-39 years 40-49 years> 50 years MEN
6-400 ng / ml 12-57 ng / mL 14-80 ng / ml 20-155 ng / ml 38-270 ng / ml 48-420 n
g / ml 30-490 ng / ml 30-530 ng / mL WOMEN 6-430 ng / ml 12-60 ng / ml 12-73 ng
/ ml 12-90 ng / ml 12-114ng/ml 12-160ng/ml 12-240ng/ml 18-340ng/ml
Ferritin is a major iron storage in the body, is a high molecular weight protein that correlates with total body stores of iron. It is found in all body cells, but mainly in the cytoplasm of reticuloendothelial cells and liver. Its
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