[Oxygen-dissociation properties and the regulation of the oxygen affinity of a hemoglobin polymer in the bull].
Oxygen-dissociation properties and some aspects of allosteric regulation of bovine hemoglobin (Hb) and its polymerized form (HbP) have been examined. It has been shown that bovine HbP as well as bovine Hb does not require the presence of organic phosphates for normal functioning and has gas transport characteristics which are similar to those of the whole human blood. Pyridoxal-5'-phosphate (PP) works as an allosteric regulator of bovine HbP only in the absence of Cl- ions and vice versa. However, in covalent binding of PP to HbP both the effectors (PP and Cl- ions) can work simultaneously and independently. Thus, by varying the Hb/PP ratio it is possible to prepare HbP solutions with preset P50 values within the range 30-55 mm Hg. The results can be used in simulation of gas transport characteristics of artificial oxygen carriers.
D000494:Allosteric Regulation; D000818:Animals; D001692:Biological Transport; D001704:Biopolymers; D002417:Cattle; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D008297:Male; D010100:Oxygen / Q000097:blood*; D010313:Partial Pressure
D001704:Biopolymers; D006454:Hemoglobins; D010100:Oxygen
Kislorodno-dissotsiatsionnye svoistva i reguliatsiia srodstva k kislorodu polimera gemoglobina byka.