Secondary structural changes in the intact and the disulfide Bridges cleaved ?-lactoglobulin A and B in solutions of urea, guanidine hydrochloride, and sodium dodecyl sulfate

1989 ◽  
Vol 8 (4) ◽  
pp. 487-494 ◽  
Author(s):  
Kunio Takeda ◽  
Yoshiko Moriyama
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Structural Changes ◽  
Guanidine Hydrochloride ◽  
Sodium Dodecyl ◽  
Disulfide Bridges ◽  
Dodecyl Sulfate

Polymer-induced structural changes in lecithin/sodium dodecyl sulfate-based multilamellar vesicles

2004 ◽  
Vol 270 (1) ◽  
pp. 187-194 ◽  
Author(s):  
Daniela Robertson ◽  
Thomas Hellweg ◽  
Brigitte Tiersch ◽  
Joachim Koetz
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Structural Changes ◽  
Sodium Dodecyl ◽  
Multilamellar Vesicles ◽  
Dodecyl Sulfate

Fractionation of nucleolar proteins by two-dimensional gel electrophoresis

1976 ◽  
Vol 54 (1) ◽  
pp. 9-14 ◽  
Author(s):  
G. Jackowski ◽  
D. Suria ◽  
C. C. Liew
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Guanidine Hydrochloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Nucleolar Proteins ◽  
Dodecyl Sulfate ◽  
Ph Range

Isolation of nucleolar proteins was obtained by dissociation in the presence of urea – guanidine hydrochloride, followed by high-speed centrifugation to remove nucleic acids. At least 31 fractions of nucleolar proteins were detected by isoelectrofocusing gel electrophoresis in the pH range 3.5–10. Following two-dimensional gel electrophoresis on sodium dodecyl sulfate – polyacrylamide slab gels, more than 100 components of nucleolar proteins were identified. Two-thirds of nucleolar proteins were located in the pH range 5–8 following isoelectrofocusing. The molecular weights of these classes of proteins were shown to be mostly 30 000 – 70 000 by sodium dodecyl sulfate – polyacrylamide gel electrophoresis.

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