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Hemoglobin proteins and

Renal Effects. Renal function tests (serum creatinine and urate, urinary hemoglobin, protein and glucose) completed in 11 hexachloroethane workers were within the normal range (Selden et al. 1994). Plasma hexachloroethane levels in these workers, who wore protective equipment, were 7.3 + 6.04 pg/L at the time of the tests (Selden et al. 1993). Mild skin and mucous membrane irritation were reported in the exposed group, suggesting that exposure may have been through either the inhalation or dermal routes of exposure. [Pg.40]

Renal Effects. No effects on renal function tests (serum creatinine and urate, urinary hemoglobin, protein and glucose) were noted in 11 hexachloroethane-exposed workers who wore protective clothing (Selden et al. 1994). [Pg.88]

Proteins may consist exclusively of a polymeric chain of amino acids these are the simple proteins. Quite often some other chemical component is covalendy bonded to the amino acid chain. Glycoproteins and Hpoproteins contain sugar and Hpid components, respectively. Porphyrins are frequently associated with proteins, eg, in hemoglobin. Proteins bound to other chemical components are called conjugated proteins. Most enzymes are conjugated proteins. [Pg.94]

Purification. Hemoglobin is provided by the red blood ceU in highly purified form. However, the red ceU contains many enzymes and other proteins, and red ceU membranes contain many components that could potentially cause toxicity problems. Furthermore, plasma proteins and other components could cause toxic reactions in recipients of hemoglobin preparations. The chemical modification reactions discussed herein are not specific for hemoglobin and may modify other proteins as well. Indeed, multifimctional reagents could actually couple hemoglobin to nonhemoglobin proteins. [Pg.166]

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. [Pg.306]

Thermodynamically it would be expected that a ligand may not have identical affinity for both receptor conformations. This was an assumption in early formulations of conformational selection. For example, differential affinity for protein conformations was proposed for oxygen binding to hemoglobin [17] and for choline derivatives and nicotinic receptors [18]. Furthermore, assume that these conformations exist in an equilibrium defined by an allosteric constant L (defined as [Ra]/[R-i]) and that a ligand [A] has affinity for both conformations defined by equilibrium association constants Ka and aKa, respectively, for the inactive and active states ... [Pg.14]

Schroeder, W. A. "Hemoglobin Structure and Function. The Proteins", H. Neurath and R. Hill, Eds., Academic Press,... [Pg.45]

Decreased red blood cell (RBC) count, hemoglobin (Hgb) and hematocrit (Hct) iron metabolism may also be altered [iron level, total iron binding capacity (TIBC), serum ferritin level, and transferrin saturation (TSAT)]. Erythropoietin levels are not routinely monitored and are generally normal to low. Urine positive for albumin or protein. [Pg.378]

The 5-iodoacetamido derivative of fluorescein (5-IAF) has been used to label numerous proteins and other biomolecules, including actin (Plank and Ware, 1987), myosin (Aguirre et al., 1986), troponin (Greene, 1986), hemoglobin (Hirsch et al., 1986), and sulfhydryl-containing proteins separated by SDS electrophoresis (Gorman, 1984). [Pg.407]

Wang, K., and Richards, F. (1975) Reaction of dimethyl-3,3 -dithiobispropionimidate with intact human erythrocytes. Cross-linking of membrane proteins and of hemoglobin. J. Biol. Chem. 250, 6622-6626. [Pg.1126]

In contrast to superoxide, which participates in one-electron transfer reactions as a reductant, nitric oxide is apparently able to oxidize various transition metal-containing proteins and enzymes. The study of NO reaction with hemoglobin has been started many years ago when... [Pg.697]


See other pages where Hemoglobin proteins and is mentioned: [Pg.21]    [Pg.389]    [Pg.615]    [Pg.21]    [Pg.389]    [Pg.615]    [Pg.330]    [Pg.200]    [Pg.2]    [Pg.396]    [Pg.14]    [Pg.45]    [Pg.113]    [Pg.287]    [Pg.122]    [Pg.200]    [Pg.150]    [Pg.180]    [Pg.286]    [Pg.30]    [Pg.86]    [Pg.409]    [Pg.584]    [Pg.615]    [Pg.173]    [Pg.1]    [Pg.336]    [Pg.246]    [Pg.1006]    [Pg.712]    [Pg.2]    [Pg.148]    [Pg.103]    [Pg.4]    [Pg.27]    [Pg.248]    [Pg.87]    [Pg.501]    [Pg.573]    [Pg.698]    [Pg.828]    [Pg.91]   
See also in sourсe #XX -- [ Pg.249 , Pg.251 ]




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Alternative Theories on How Hemoglobins and Other Allosteric Proteins Work

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