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.
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 76, No. 4, pp. 564–570, July–August 2009.
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Vlasova, I.M., Saletsky, A.M. Study of the denaturation of human serum albumin by sodium dodecyl sulfate using the intrinsic fluorescence of albumin. J Appl Spectrosc 76, 536–541 (2009). https://doi.org/10.1007/s10812-009-9227-6
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DOI: https://doi.org/10.1007/s10812-009-9227-6