[Physico-chemical properties and thermostability of human hemoglobin molecules modified by rheopolyglucin and dialdehydedextrane].
The structural characteristics and thermostability of human hemoglobin molecules modified by rheopolyglucin and dialdehydedextrane have been studied. The influence of mixture pH, the exposure time, and temperature of incubation and the rate of dextrane oxidation on the intensity of conjugation of human hemoglobin with dialdehydedextrane has been estimated. Optimal conditions for the binding of hemoglobin to dialdehydedextrane have been determined. The formation of the hemoglobin- dialdehydedextrane complex leads to the shielding of protein chromophore groups by the polysaccharide matrix and the transformation of a part of hemoproteid molecules from the low-spin form (HbO2) to high-spin forms (Hb, MetHb). It has been found that the temperature of denaturation transition for the native protein and hemoglobin in the presence of rheopolyglucin is 60 degrees C, and that for the hemoglobin-dialdehydedextrane conjugate is 80 degrees C. The latter is probably determined by the enhancement of hydrophobic interactions inside the protein globule under the effect of dialdehydedextrane and by the ability of the externally-bound carbohydrate components to prevent the association of hemoglobin molecules.
Artiukhov
V G
VG
Putintseva
O V
OV
Savostin
V S
VS
D002850:Chromatography, Gel; D003911:Dextrans / Q000737:chemistry*; D006361:Heating; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008027:Light; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D012542:Scattering, Radiation; D012996:Solutions; D013438:Sulfhydryl Compounds / Q000737:chemistry
D003911:Dextrans; D006454:Hemoglobins; D008024:Ligands; D012996:Solutions; D013438:Sulfhydryl Compounds; C026948:dextran dialdehyde