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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1969-1-5
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pubmed:abstractText |
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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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/Coloring Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lactoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Methemoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Myoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Ovalbumin,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroglobulin,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Globulins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
109
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
825-30
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:4177067-Catalase,
pubmed-meshheading:4177067-Coloring Agents,
pubmed-meshheading:4177067-Detergents,
pubmed-meshheading:4177067-Dialysis,
pubmed-meshheading:4177067-Glycoproteins,
pubmed-meshheading:4177067-Lactoglobulins,
pubmed-meshheading:4177067-Methemoglobin,
pubmed-meshheading:4177067-Molecular Weight,
pubmed-meshheading:4177067-Muramidase,
pubmed-meshheading:4177067-Myoglobin,
pubmed-meshheading:4177067-Ovalbumin,
pubmed-meshheading:4177067-Oxidation-Reduction,
pubmed-meshheading:4177067-Protein Binding,
pubmed-meshheading:4177067-Proteins,
pubmed-meshheading:4177067-Ribonucleases,
pubmed-meshheading:4177067-Serum Albumin, Bovine,
pubmed-meshheading:4177067-Sodium,
pubmed-meshheading:4177067-Solubility,
pubmed-meshheading:4177067-Sulfates,
pubmed-meshheading:4177067-Thyroglobulin,
pubmed-meshheading:4177067-Time Factors,
pubmed-meshheading:4177067-gamma-Globulins
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pubmed:year |
1968
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pubmed:articleTitle |
The binding of sodium dodecyl sulphate to various proteins.
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pubmed:publicationType |
Journal Article
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