Journal
JOURNAL OF APPLIED SPECTROSCOPY
Volume 76, Issue 4, Pages 536-541Publisher
SPRINGER
DOI: 10.1007/s10812-009-9227-6
Keywords
fluorescence; tryptophan; human serum albumin; denaturation; sodium dodecyl sulfate
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Funding
- Russian Foundation for Basic Research [07-02-00459]
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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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