Luminescent spectral characteristics of eosin in solutions of human serum albumin when denatured by treatment with sodium dodecyl sulfate

2006 ◽  
Vol 73 (5) ◽  
pp. 743-747 ◽  
Author(s):  
I. M. Vlasova ◽  
A. Yu. Zemlyanskii ◽  
A. M. Saletskii
Keyword(s):  
Human Serum Albumin ◽  
Sodium Dodecyl Sulfate ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectral Characteristics ◽  
Sodium Dodecyl ◽  
Dodecyl Sulfate

Microheterogeneity of human serum albumin: evidence for differences in reducibility of disulfide linkages

1968 ◽  
Vol 46 (8) ◽  
pp. 789-795 ◽  
Author(s):  
A. F. S. A. Habeeb
Keyword(s):  
Human Serum Albumin ◽  
Sodium Dodecyl Sulfate ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Free Amino ◽  
Sodium Dodecyl ◽  
Amino Groups ◽  
Trinitrobenzenesulfonic Acid ◽  
Disulfide Linkages

Studies were designed to determine the causes of the microheterogeneity of human serum albumin. Human serum albumin in 3 M KCl was fractionated in a stepwise manner by lowering the pH. The resultant fractions showed similarities in: (a) the reactivity of ε-amino groups with trinitrobenzenesulfonic acid, (b) the binding of sodium dodecyl sulfate to the free amino groups, and (c) the ability to precipitate with anti-human serum albumin. Conversely, differences existed in the susceptibility to reduction of disulfide bonds of the various fractions with β-mercaptoethanol, which suggested that the microheterogeneity of human serum albumin and its fraction may be due, in part at least, to differences in the pairing of the disulfide bonds.

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