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The Binding of Sodium Dodecyl Sulphate to Various Proteins

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Journal Biochem J
Specialty Biochemistry
Date 1968 Oct 1
PMID 4177067
Citations 81
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Abstract

1. The binding of sodium dodecyl sulphate to proteins by equilibrium dialysis was investigated. 2. Most of the proteins studied bound 90-100% of their weight of sodium dodecyl sulphate. 3. The glycoproteins studied bound 70-100% of their weight of sodium dodecyl sulphate, calculated in terms of the polypeptide moiety of the molecule. 4. Proteins not containing S.S groups bound about 140% of their weight of sodium dodecyl sulphate. 5. Reduction of four proteins containing S.S groups caused a rise in sodium dodecyl sulphate binding to 140% of the weight of protein. 6. The apparent micellar molecular weights of the protein-sodium dodecyl sulphate complexes were measured by the dye-solubilization method; they were all found to have approximately the same micellar molecular weight (34000-41000) irrespective of the molecular weight of the protein to which they were attached.

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References
1.
CREETH J, Knight C . The macromolecular properties of blood-group substances. Sedimentation-velocity and viscosity measurements. Biochem J. 1967; 105(3):1135-45. PMC: 1198435. DOI: 10.1042/bj1051135. View

2.
Pusztai A, Morgan W . STUDIES IN IMMUNOCHEMISTRY. 22. THE AMINO ACID COMPOSITION OF THE HUMAN BLOOD-GROUP A, B, H AND LE-A SPECIFIC SUBSTANCES. Biochem J. 1963; 88:546-55. PMC: 1202214. DOI: 10.1042/bj0880546. View

3.
EDELHOCH H, LIPPOLDT R . The properties of thyroglobulin. II. The effects of sodium dodecyl sulfate. J Biol Chem. 1960; 235:1335-40. View

4.
Habeeb A, CASSIDY H, Singer S . Molecular structural effects produced in proteins by reaction with succinic anhydride. Biochim Biophys Acta. 1958; 29(3):587-93. DOI: 10.1016/0006-3002(58)90016-7. View

5.
Reynolds J, Herbert S, Polet H, Steinhardt J . The binding of divers detergent anions to bovine serum albumin. Biochemistry. 1967; 6(3):937-47. DOI: 10.1021/bi00855a038. View