An analysis of the intrinsic tryptophan fluorescence of human serum albumin (HSA) confirms that the denaturation of HSA by sodium dodecyl sulfate takes place in two stages for different pH levels: the first is the disintegration of globules and the second is the complete unfolding of the amino acid chain of HSA. At pH levels below the isoelectric point (pI 4.7) of HSA, denaturation proceeds through both stages, but when the pH is above pI, denaturation ceases in the first stage.
Raman spectroscopy method is applied for analysis of ischemia damaging action on serum. The registered changes of low-density lipoprotein (LDL) after brain ischemia (size increasing, density reducing) are explained in frameworks of free radical theory of oxidative stress. We confirmed by Raman spectroscopy method our hypothesis, according to which the increase in LDL size and decrease of LDL density after an ischemia, in contrast to LDL of healthy animals, is caused by loosing of LDL phospholipid monolayer under damaging action of free radicals. The obtained results show the possibility of using of Raman spectroscopy method for an estimation of ischemic damages. Averaged Raman spectrum of blood serum of healthy animals and animals after ischemia
The mechanism of binding of molecular probe fluorescein to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding Center on human serum albumin molecule for fluorescein is determined. The amino acid residues of albumin molecule, participating in binding of fluorescein at different pH values of solution, are established. The conformation rearrangements of globules of human serum albumin, taking place at binding of fluorescein at different pH values of solution, are registered.
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