[Effect of rheopolyglucin and dialdehyde dextran on thermostability of human haemoglobin molecules].
Structural characteristics and thermostability of human haemoglobin molecules, modified by reopolyglukine and dialdehyddextrane (DAD) have been studied. Haemoglobin mainly preserves its oxyform when including reopolyglukine in mixture (the mol. ratio of protein to dextrane was 1:4), and disordering of polypeptide chains and increasing the volume of haemoproteids molecules are noticed. Assessment of the influence of mixture pH, exposure and temperature of incubation and the rate of dextrane oxidation on the intensity of the process of human haemoglobin conjugation with DAD have been chosen. Formation of the haemoglobin-DAD complex leads to shielding protein chromophoral groups by polysugar matrix and to transforming the part of haemoproteid molecules from lowspin form (HbO2) to highspin forms (Hb, MetHb). It has been detected that temperature of denaturational points for native protein and haemoglobin in the presence of reopoliglukine is 60 degrees C, but it is 80 degrees C for the haemoglobin-DAD conjugate. The latter is probably determined by increasing hydrophobic interactions inside the protein globule under the effect of DAD and by ability of the surface-bound carbohydrate components prevent association of haemoglobin molecules.
Artiukhov
V G
VG
Putintseva
O V
OV
Savostin
V S
VS
D003911:Dextrans / Q000494:pharmacology*; D006454:Hemoglobins / Q000737:chemistry*; D006358:Hot Temperature; D006801:Humans; D010952:Plasma Substitutes / Q000494:pharmacology*; D011489:Protein Denaturation
D003911:Dextrans; D006454:Hemoglobins; D010952:Plasma Substitutes; C026948:dextran dialdehyde