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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1021/la103360h
|2 doi
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|a pubmed25n0675.xml
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|e rakwb
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|a eng
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1 |
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|a Noskov, B A
|e verfasserin
|4 aut
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|a Bovine serum albumin unfolding at the air/water interface as studied by dilational surface rheology
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a Date Completed 04.03.2011
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|a Date Revised 16.11.2017
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Measurements of the surface dilational elasticity close to equilibrium did not indicate significant distinctions in the surface conformation of different forms of bovine serum albumin (BSA) in a broad pH range. At the same time, the protein denaturation in the surface layer under the influence of guanidine hydrochloride led to strong changes in the kinetic dependencies of the dynamic surface elasticity if the denaturant concentration exceeded a critical value. It was shown that the BSA unfolding at the solution surface occurred at lower denaturant concentrations than in the bulk phase. In the former case, the unfolding resulted in the formation of loops and tails at surface pressures above 12 mN/m. The maximal values of the dynamic surface elasticity almost coincided with the corresponding data for the recently investigated solutions of β-lactoglobulin, thereby indicating a similar unfolding mechanism
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Lactoglobulins
|2 NLM
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|a Solutions
|2 NLM
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|a Water
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|a 059QF0KO0R
|2 NLM
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|a Serum Albumin, Bovine
|2 NLM
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| 650 |
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|a 27432CM55Q
|2 NLM
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|a Mikhailovskaya, A A
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|a Lin, S-Y
|e verfasserin
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|a Loglio, G
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|a Miller, R
|e verfasserin
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 26(2010), 22 vom: 16. Nov., Seite 17225-31
|w (DE-627)NLM098181009
|x 1520-5827
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| 773 |
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|g volume:26
|g year:2010
|g number:22
|g day:16
|g month:11
|g pages:17225-31
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|u http://dx.doi.org/10.1021/la103360h
|3 Volltext
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