[Parameters of oxygen-binding function of human hemoglobin modified by carbon oxide and UV-light].
The parameters of oxygen-binding function of human hemoglobin, modified by carbon oxide and UV-radiation: the pressure of half-saturation with the ligand (P50), Hill's constant (n), and arterial-venous difference of HbO2 concentration in the sample were studied. The presence of carboxyform in blood in boundaries of admissible values (lower than 10 per cents) did not noticeably influence to the oxygenation parameters. Functional properties of hemoproteid were substantially modified in case of HbCO concentration increasing from 30 up to 80 percent. It has been discovered, that the leading mechanism of protection from hemic hypoxia in case of poisoning with CO is decreasing of degree of cooperative interactions and relative affinity of hemoglobin for ligands. The stimulating influence of UV-light to the functional properties of modified with carbon oxide human hemoglobin observed in case carboxyform hemoprotein concentration in solution was lower than 10 percent. The disturbance of oxygen-binding ability of hemoglobin at the influence of higher concentrations of Hb-CO was inconvertible and was not correct with UV-radiation.
Artiukhov
V G
VG
Kalaeva
E A
EA
Putintseva
O V
OV
Preobrazhenskiĭ
A P
AP
D002245:Carbon Dioxide / Q000378:metabolism; D002263:Carboxyhemoglobin / Q000378:metabolism* / Q000528:radiation effects*; D006454:Hemoglobins / Q000378:metabolism* / Q000528:radiation effects*; D006801:Humans; D010100:Oxygen / Q000378:metabolism*; D010108:Oxyhemoglobins / Q000378:metabolism / Q000528:radiation effects; D011485:Protein Binding; D014466:Ultraviolet Rays
D006454:Hemoglobins; D010108:Oxyhemoglobins; D002245:Carbon Dioxide; D002263:Carboxyhemoglobin; D010100:Oxygen