Metal-catalyzed oxidation of human serum albumin does not alter the interactive binding to the two principal drug binding sites
It is well known that various physiological factors such as pH, endogenous substances or post-translational modifications can affect the conformational state of human serum albumin (HSA). In a previous study, we reported that both pH- and long chain fatty acid-induced conformational changes can alte...
Main Authors: | , , , , , |
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Format: | Article |
Language: | English |
Published: |
Elsevier
2018-07-01
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Series: | Biochemistry and Biophysics Reports |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580818300268 |