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Hemoglobin functions

D. Agents which act on the blood or hematopoietic system Decreases hemoglobin function deprive body tissues of oxygen ... [Pg.182]

Skin rash followed by blistering Interferes with blood hemoglobin functioning Dry land drowning Asphyxiation Heart failure... [Pg.111]

While hemoglobin adduct formation does not imply altered or abnormal hemoglobin function, adduct formation may be a suitable biomarker of human exposure to 3,3 -dichlorobenzidine (see Section 2.7). Hematological variables (erythrocyte count, hemoglobin concentration, hematocrit, and leucocyte count) were found to be normal in dogs exposed to 10.4 mg/kg/day 3,3 -dichlorobenzidine for 7 years (Stula et al. 1978). [Pg.45]

A number of copper -containing protein compounds are enzymes with an oxidase function (ascorbic acid oxidase, urease, etc 1 and these play an important role in Ihe biological oxidation-reduction system. There is a definite relationship of copper with iron in connection with utilization of iron in hemoglobin function. [Pg.442]

One must marvel at the way various factors work in concert so that hemoglobin can be useful in multiple roles oxygen deliverer, carbon dioxide remover, and pH stabilizer. From the explanation we have given it should be clear why the hemoglobin is confined to cells in the blood rather than being present as a free plasma protein. The intracellular carbonic anhydrase and GBP of the erythrocytes are essential for efficient hemoglobin function. [Pg.104]

Clementi, M.E., S.G.Condo, M. Castagnola, and B. Giardina (1994). Hemoglobin function under extreme life conditions. Eur. J. Biochem. 223 309-317. [Pg.152]

Poyart, C., H. Wajcman and J. Kister (1992). Molecular adaptation of hemoglobin functions in mammals. Resp. Physiol. 90 3-17. [Pg.155]

Bunn, H.F. Hemoglobin function in stored blood. J Clin Invest. 1969, 48, 311-321. [Pg.373]

The toxicity of antimony is a function of the water solubility and the oxidation state of the antimony species under consideration. It can react with red cell membrane and interfere with hemoglobin function. It has high affinity for sulfhydryl groups. [Pg.150]


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See also in sourсe #XX -- [ Pg.1249 , Pg.1254 , Pg.1255 , Pg.1256 , Pg.1257 , Pg.1258 ]




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