作者: Michelle R. Baker , Sean K. Benton , Christopher S. Theisen , Chad A. McClintick , Eugene E. Fibuch
DOI: 10.1155/2011/739712
关键词: Biophysics 、 Human serum albumin 、 Bioinformatics 、 Methylglyoxal 、 Protein structure 、 Chemical modification 、 Chemistry 、 Isoflurane
摘要: Persistent alteration of protein conformation due to interaction with isoflurane may be a novel molecular aspect preconditioning. We preincubated human serum albumin isoflurane, dialyzed release agent, and assessed conformation. Susceptibility chemical modification by methylglyoxal nitrophenylacetate was also examined. Isoflurane had persistent effect on An increase in the susceptibility surface residues attended this change Modification isoflurane-treated HSA included intra- intersubunit cross-linking that consequence anesthetic-induced changes multimeric subpopulations. This irreversible represent mechanism for