Hemoglobins carbon monoxide

HbCO Carbon monoxide hemoglobin Leu Leucine or leucyl... 

Solubility of horse carbon monoxide hemoglobin in different salt solutions. The addition of a moderate amount of salt (salting in) is required to solubilize this protein. At high concentrations, certain salts compete more favorably for solvent, decreasing the solubility of the protein and thus leading to its precipitation (salting out). (Source-. E. J. Cohn and J. T. Edsall, Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions. Copyright 1942, Reinhold, New York, N.Y.)... 

Carbon monoxide hemoglobin Oxyhemoglobin High-density lipoprotein Histidine... 

The absorbance change with carbon monoxide hemoglobin (HbCO) is demonstrated in Fig. 13 as a result obtained by Noe et al.57). In this experiment a modelocked Nd glass laser at 530 nm (6 ps) was applied as excitation source. The data were displayed in the form AA, change in absorbance between excitation and no excitation, versus time (Fig. 13). 

PI. Paul, E. G., and Thorell, H., A colorimetrical carbon-monoxide-hemoglobin method of determination for clinical use. Acta Physiol. Scand. 4, 285 (1942). 

An example of the above occurs when human carbon monoxide hemoglobin is eleetrofoeused in a pH gradient 6-8. It exhibits droplet sedimentation in the middle zones if a total protein amount of 1.5 mg/cm of cross section has been added at the start. In the LKB 110 ml column this corresponds to about 8 mg. The same amount of protein electro-focused in a pH-gradient of 7-8 does not show droplet sedimentation. 

Carbonmonoxyhemoglobin, carbon monoxide hemoglobin (carboxyhemt obin) a compound of ferrohemoglobin and carbon monoxide. 

The pH dependence of the Cl excess line width in solutions of carbon monoxide hemoglobin and deoxy hemoglobin was studied in the pH range 4.8 to 10.5. The results are shown in Fig. 8.19. (Carbon mono-... 

Fig. 8,19. Cl excess line width as a function of pH in a solution of human oxy and carbon monoxide hemoglobin in 0.5 M NaCl. Key to the symbols O, refers to carbon monoxide hemoglobin o, refers to deoxy hemoglobin. The line widths shown are normalized to a hemoglobin concentration of 2.5 % by weight. (After Chiancone et al, [466])...

Carbon monoxide is a chemical asphyxiant and acts toxically by combining with the hemoglobin of the red blood cells to form the stable compound carbon monoxide-hemoglobin. It thus prevents the hemoglobin from taking up... 

As we have said, n striking contrast to hemoglobin itself both carbon monoxide hemoglobin and oxyhemoglobin are diamagnetic, the bonding being completely covalent (146). In both compounds the iron porphyrin... 

M NaCl. Circles carbon monoxide hemoglobin. Squares deoxyhemoglobin. With permission from Ref. 89. Copyright Academic Press Inc. (London) Ltd. 

Reduction of the peroxidase with hydrosulfite gives a red solution of ferroperoxidase with the bands 694.5 (narrow) and 558 mp (broad and flat). On shaking with air the ferroperoxidase is reoxidized, apparently without the formation of an oxyferrous compound. It thus differs in this respect from hemoglobin. The ferroperoxidase gives a red carbon monoxide compound with two bands at 678 and 545.5 mp. The intensity and size resemble the bands of carbon monoxide hemoglobin, but are displaced 8 mp toward the red. 

Differential titration experiments were carried out on three systems (79). Ferroperoxidase and carbon monoxide ferroperoxidase gave identical curves. The peroxidase thus shows no Bohr effect. Since the two derivatives correspond as to bond types to the analogous hemoglobin and carbon monoxide hemoglobin, it can be stated with fair certainty that the heme-linked groups in horse-radish peroxidase are not imidazole. 

It may be noticed that while the observed values of the dissociation constants and .3 differ from the hypothetical values by a factor less than 10, the observed value of ,4 is 3 X 10 times smaller than the corresponding value expected in the absence of heme-heme interaction. This large discrepancy suggests the stabilization due to some possible structural change when the hemoglobin molecule is fully oxygenated. Similar discrepancy was found in the dissociation of carbon monoxide hemoglobin. 

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