Influence of Binding of Sodium Dodecyl Sulfate, All-trans-retinol, and 8-Anilino-1-naphthalenesulfonate on the High-Pressure-Induced Unfolding and Aggregation of β-Lactoglobulin B

2005 ◽  
Vol 53 (20) ◽  
pp. 8010-8018 ◽  
Author(s):  
Thérèse Considine ◽  
Harjinder Singh ◽  
Hasmukh A. Patel ◽  
Lawrence K. Creamer
Langmuir ◽  
2000 ◽  
Vol 16 (21) ◽  
pp. 8176-8181 ◽  
Author(s):  
Alan R. Mackie ◽  
A. Patrick Gunning ◽  
Peter J. Wilde ◽  
Victor J. Morris

1968 ◽  
Vol 46 (6) ◽  
pp. 625-627 ◽  
Author(s):  
James Leslie ◽  
Frederick Varricchio

The rate of oxidation of β-lactoglobulin with ferricyanide decreases markedly as the concentration of sodium dodecyl sulfate is increased from 0.25 to 1.0%, whereas the detergent concentration has little effect on the rate of oxidation of this protein by o-iodosobenzoate and 2,6-dichlorophenol indophenol. It is suggested that the structure of this protein in sodium dodecyl sulfate, coupled with the steric effect of bound detergent molecules, hinders the formation of a transition state involving the sulfhydryl group, a heavy metal ion, and the ferricyanide ion.


2008 ◽  
Vol 9 (9) ◽  
pp. 2477-2486 ◽  
Author(s):  
Jin-Mi Jung ◽  
Gabriela Savin ◽  
Matthieu Pouzot ◽  
Christophe Schmitt ◽  
Raffaele Mezzenga

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