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Study on Dissociation of Pig Hemoglobin Molecules Induced by Urea and Guanidine Hydrochloride(cas 50-01-1)

The dissociation process of porcine hemoglobin induced by urea and guanidine hydrochloride(cas 50-01-1) was studied by using endogenous fluorescence spectroscopy, non-denaturing polyacrylamide gel electrophoresis and high efficiency gel exclusion chromatography.

Based on the thermodynamic equilibrium of the interaction between denaturant molecules and porcine hemoglobin molecules, a theoretical model for quantifying the dissociation process of pig hemoglobin molecules induced by denaturant was established based on the mutual association and dissociation balance between them. Through this theoretical model, two characteristic parameters k and m, which describe the transformation between the various subunits during the dissociation of porcine hemoglobin molecules, can be obtained, where k represents the dissociation of porcine hemoglobin molecules from one subunit state to another the thermodynamic equilibrium constant of the subunit state, m represents the number of denaturant molecules that are averaged in each swine hemoglobin subunit molecule.

In the process of dissociation of porcine hemoglobin molecules induced by porcine hemoglobin, part of the porcine hemoglobin molecule is dissociated into a dimer by tetramer when the denaturant concentration is greater than or equal to 5.0 mol / L in the solution, and the content of the dimer varies with the solution. The k and m of the dissociation process were 4.18 × 10-9 L · mol-1 and 1.69, respectively. In the process of dissociation of porcine hemoglobin induced by guanidine hydrochloride(cas 50-01-1), when the concentration of the denaturant was increased, when the denaturant concentration is greater than or equal to 3.5 mol /L, part of the porcine hemoglobin molecule is dissociated into a dimer by tetramer and further dissociated into a monomer. As the concentration of guanidine hydrochloride(cas 50-01-1) in the solution increases, the monomer content gradually increases. The dimer content gradually decreased, the tetramer content did not change much, the dissociation process k1, k2 were 7.82 × 10-7L · mol-1,3.56 × 10-9L · mol-1, m1, and m2 were 1.17 and 3.06 respectively. By comparing the dissociation process of porcine hemoglobin and the characteristic parameters k and m induced by guanidine hydrochloride, the induced dissociation ability of guanidine hydrochloride was stronger than that of urea. At the same time, by comparing the changes of porcine hemoglobin molecules in different concentrations of urea and guanidine hydrochloride solution, the activity of porcine hemoglobin molecules changed faster than their structural changes.

 

 

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