[Mathematical models of the oxygen-binding function of intact human hemoglobin and hemoglobin modified by UV-radiation in the presence of carbon oxide].
The influence of carbon oxide and UV-radiation in doses of 151-453 J/m2 on the physiological properties of human oxyhemoglobin has been studied. Mathematical models of the oxygen-binding function of intact and modified hemoprotein have been developed. It has been found that saturation of human hemoglobin with oxygen obeys the logistic dependence. In the presence of carboxyhemoglobin, the oxygenation parameters change and saturation curves are described by the equations of degree dependence. It has been shown that UV light had the stimulating influence on the functional properties of human hemoglobin modified by carbon oxide if the concentration of carboxyform of the hemoprotein in solution was no higher than 10 per cent. The disturbance of the oxygen-binding ability of hemoglobin by the action of higher concentrations of carboxyhemoglobin was irreversible and was not corrected by UV-radiation.
Artiukhov
V G
VG
Kalagaeva
E A
EA
Putintseva
O V
OV
Preobrazhenskiĭ
A P
AP
D002245:Carbon Dioxide / Q000737:chemistry* / Q000378:metabolism; D002263:Carboxyhemoglobin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008956:Models, Chemical; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism; D010108:Oxyhemoglobins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding / Q000528:radiation effects; D014466:Ultraviolet Rays
D010108:Oxyhemoglobins; D002245:Carbon Dioxide; D002263:Carboxyhemoglobin; D010100:Oxygen