[Effect of chemical modification of hemoglobin on its biological activity].
Oligomeric hemoglobins were produced after polycondensation with glutaric aldehyde (OHb) as well as after modification with pyridoxal-5-phosphate (OHb-PLP). OHb exhibited high affinity to oxygen (P50 = 17 torr) as well as a decreased rate of the subunits cooperative interaction (n = 1.5-1.6); OHb-PLP possessed P50 = 27 torr, n = 2.2 (for pO2 greater than P50), Bore effect -0.4. The P50 pattern was not distinctly altered in presence of approximately 15% Met hemoglobin, while already 8% of the Met form affected the "n" parameter. Biological activity of OHb and OHb-PLP was studied.
Gudkin
L R
LR
Kuznetsova
N P
NP
Samsonov
G V
GV
Mishaeva
R N
RN
Stragovich
L M
LM
D001802:Blood Substitutes; D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000378:metabolism*; D010313:Partial Pressure
D001802:Blood Substitutes; D006454:Hemoglobins; D010108:Oxyhemoglobins; D010100:Oxygen
Vliianie khimicheskoĭ modifikatsii gemoglobina na ego biologicheskuiuaktivnost'.