Hemoglobin formation

Lungs saturated with oxygen so the shift is to oxyhemoglobin formation. Tissues low in oxygen, so in venal blood, the shift is to hemoglobin formation. 

Endpoint/Concentration/Rationale Because the exposures did not result in effects consistent with the definition of an AEGL-3, the concentration vs percent hemoglobin formation data presented by the authors was graphed and projected to a methemoglobin level of 70-80%, which was considered the threshold for lethality in humans. This value was approximately 250 ppm. An 8-h exposure to 250 ppm was chosen as the basis for the AEGL-3 calculations. 

Luchsinger BP, Rich EN, Gow AJ, Williams EM, Stamler JS, Singel DJ. Routes to S-nitroso-hemoglobin formation with heme redox and preferential reactivity in the beta subunits. Proc. Natl. Acad. Sci. U. S. A. 2003 100 461-466. 

Smith, E. W., and Torbert, J. V., Study of two abnormal hemoglobins with evidence for a new genetic locus for hemoglobin formation. Bull. Johns Hopkins Hosp. 102, 38-45 (1958). 

Gerok W, Waller HD. Hamoglobinbildung durch Furadantin. [Hemoglobin formation by furadantin (N-[5-nitro-2-furfuryliden]-l-aminohydantoin).j Dtsch Med Wochenschr 1956 81(43) 1707-9. 

However, the hemoglobin response of rats fed a diet that contained diferric phytate was only slightly better than that supported by the low iron basal diet. The response to the tetra-ferric phytate was intermediate between responses to the di- and monoferric phytate. The bioavailabilities of the iron of the three ferric phytates are markedly different. In another experiment (10), a 60-fold excess of phytic acid as sodium phytate did not depress the ability of monoferric phytate to support hemoglobin formation in growing rats. 

Ellis and Morris (12) tested the ability of an insoluble calcium-iron-phytate product to support hemoglobin formation in growing rats. The product had an approximate molar composition of CajFe phytate. After a 3-week feeding period the hemoglobin concentration of rats fed monoferric phytate was 2.7 g/dl greater than for rats fed the insoluble calcium-ferric-phytate product the difference was significant at P<0.05. 

Necessary for iron utilization and hemoglobin formation constituent of cytochrome oxidase involved in bone and elastic tissue development... 

The parameters are defined next. First defined is the rate of hemoglobin formation as a nonlinear function. Then the rate of endogenous erythropoietin is defined. 

Schultze, M. 0., Elvehjem, C. A., and Hart, E. B., Further studies on the availability of copper from various sources as a supplement to iron in hemoglobin formation. J. Biol. Chem. 116, 453-457 (1936). 

Upon entering the bloodstream the iron is immediately bound by a plasma protein denoted as a Pj-globuhn, called transferrin (siderophilin). The transferrin-bound iron is utilized for hemoglobin formation via reticnlocytes. 

USE Photographic developer intermediate in the manufacture of sulfur and azo dyes in dyeing furs and feathers. Caution May cause skin sensitization, dermatitis, Inhalation can cause asthma, met hemoglobin formation. 

Young rats fed on milk alone failed to gain in weight and developed anemia, Cu restored erythrocyte hemoglobin formation... 

Interest in the biological role of copper has greatly increased as the recognition of its role in a number of key physiological processes has developed. These include its importance in elastin and collagen formation which prevent aneurisms, soft bones, and other defects 1,2), the requirement for copper in the taste response (3), and its requirement for cytochrome oxidase and related systems 4). Finally, there is perhaps the best known biological role of copper— its involvement in hemoglobin formation (5, 6, 7). I propose to deal exclusively with the latter, the role... 

Since 1926, it has been known that large quantities of partially cooked liver can help cure pernicious anaemia. This is an often fatal, complex disease, in which there is a deficiency in red cells and hemoglobin formation. 

Copper Drinking water, Uver, grains, legumes, nuts Component of numerous enzymes, hemoglobin formation Anemia, fragility of arteries... 

Vitamin Bg is essential for more than 100 enzymes involved in protein metabolism. Pyridoxal-5 -phosphate is covalently bound to enzymes via a SchifFs base with an e-amino group of lysine in the enzyme. PLP-dependent enzymes are involved in important steps of amino acid metabolism, hemoglobin formation and chlorophyll biosynthesis. Vitamin Bg could have a role in preventing oxidative stress of the cells and is an impotent quencher of singlet oxygen. 

Later hematotoxicity 40-45 Hemoglobin formation impaired via heme and globin effects U.S. ATSDR (1988,. 2007)... 

As may be surmised from its chemical composition, ferritin is used as a source of iron to be used for hemoglobin formation and to store liberated iron ensuing from the destruction of hemoglobin. Evidence for such an assumption can be found in the following experiments carried out with radioactive iron (9). 

If nitric oxide is inhaled, remove the individual to fresh air and get immediate medical attention. If breathing is difficult, administer oxygen. If breathing has stopped, give artificial respiration. Keep the person warm and quiet. Keep victims under competent medical observation for 48 to 72 hours or until the hazard of delayed pulmonary edema has passed. First aid in treating met-hemoglobin formation involves the administration of oxygen. 

As a result of a series of studies beginning in 1925 (and reported in 1928), Hart and associates at the University of Wisconsin discovered that a small amount of copper is necessary, along with iron, for hemoglobin formation. Then, in 1931, Josephs found that copper was more effective than iron alone in overcoming the anemia of milk-fed infants. Today, copper is considered as an essential nutrient for all vertebrates and some lower animal species. 

Lamb is important in the diet, not for its appetite appeal alone, but for the essential food nutrients that it contains. It is an excellent source of high-quality protein for muscle building and body maintenance. In most cuts of lamb, the fat may be easily separated from the lean hence, the calories can be adjusted to desired levels. Lamb is one of the best sources of iron, needed for hemoglobin formation and it is rich in phosphorus, needed for bones and teeth. It is also an excellent source of vitamin B-12, vitamin B-6, biotin, niacin, pantothenic acid, and thiamin. Also, lamb muscle is easily digested, so it is included in the diet of both the young and aged. 

Hemoglobin formation. It is necessary for the formation of a precursor of porphyrin compounds which is part of the hemoglobin molecule. 

The labeling technique has been used to study the life-span of erythrocytes in patients with anemias and porphyrias (343, 359). In a hemolytic anemia patient most of the labeled stercobilin was found to be excreted some 20 days after feeding of labeled glycine. In sickle cell anemia it was concluded that a random destruction of erythrocytes took place to compensate for this destruction the rate of hemoglobin formation was nearly tripled. In pernicious anemia an abnormal pattern of erythrocyte destruction was also found but the erythrocyte life-span returned to normal after liver therapy. 

Cyanocobalamin (Bjj), which is not present in grains and vegetables, also acts as a coenzyme, especially in bone marrow, neurons, and gastrointestinal epithelial cells. It is involved in hemoglobin formation, and plays a major role in the prevention of pernicious or macrocytic anemia (fewer and larger red blood cells than normal) and the maintenance of nerve tissues. The acute deficiency can also cause mental disorders. It is important to point out that cyanocobalamin is the only vitamin that requires a specific factor for its absorption. This factor is called intrinsic castle and is a muco- or glycoprotein secreted by the stomach. 

Porphin synthesis occurs at a rapid rate in two places, namely, in the immature red blood cell and in the etiolated plant leaf cell exposed to light. The first evidence of hemoglobin formation is observed in the polychroma-... 

In the heme-repleted cell, the synthesis of a and of yS chains is stimulated approximately to the same degree. Excess a chain synthesis and the a pool are maintained, but heme appears to facilitate the combination of newly synthesized a and /8 chains immediately prior to or after their release from the polyribosomes (pathway 1). This effect of heme serves to bypass the a pool. In this manner, heme may be said to coordinate the synthesis of a and y8 chains. The ayS pool disappears by combination with heme pathway 4 is accelerated and hemoglobin formation is enhanced. 

Levere, R. D., and Granick, S. (1965). Control of hemoglobin synthe.sis in the cultured chick blastoderm by delta-aminolevulinic acid synthetase increase in the rate of hemoglobin formation with delta-aminolevulinic acid. Proc. Natl. Acad. Sci. U.S. 54, 134-137. 

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