Abstract
Abstract The interaction of sodium dodecyl sulfate with a wide variety of proteins is characterized by a high binding ratio when the monomer concentration of amphiphile exceeds 5 x 10-4 m. This binding ratio on a gram to gram basis is identical for all proteins investigated. The protein portion of the complex contains a high degree of order, and hydrodynamic studies suggest that the complex is a rodlike particle, the length of which varies uniquely with the molecular weight of the protein moiety. These results explain the empirical observation that proteins dissolved in aqueous solutions containing high concentrations of sodium dodecyl sulfate have electrophoretic mobilities on polyacrylamide gels which are a unique function of their molecular weights. In addition, the data suggest a possible model for the conformation of membrane proteins and their interactions with phospholipid.
Highlights
We have demonstrated that a wide variety of reduced proteins bind identical amounts of SDS on a gram to gram basis when the equilibrium monomer concentration of amphiphile is greater than 5 X lop4 M [2]
:Mater&---The proteins used and their sources are shown in Sodium dodecyl sulfate was a highly pure grade obtained from Mann
The interaction between these proteins and the lipid is thought to be coulombic in the case of cytochrome c and through a ternary Mg+f complex in the case of the bacterial ATPase
Summary
Mater&---The proteins used and their sources are shown in Sodium dodecyl sulfate was a highly pure grade obtained from Mann. Preparation of Protein-SDS &‘omplexes-Protein was dissolved in 6 M GuHCl and 0.1% P-mercaptoethanol to obtain polypeptide chains in the random coil conformation [9]. The GuHCl was removed by dialysis against Hz0 containing a reducing agent. SDS, P-mercaptoethanol, and the appropriate buffer were dialyzed into the bag containing the protein solution. The amount of bound SDS and the.concentration of protein were determined as described previously [2]. It has been demonstrated that the same final binding ratio is reached when the complex is obtained by the above procedure as when it is formed by treating the native protein directly with SDS and P-mercaptoethanol
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