A low-angle laser light scattering study of the association behavior of a major membrane protein of Rhodospirillum rubrum chromatophore at various concentrations of sodium dodecyl sulfate where polypeptides derived from water-soluble globular proteins are solubilized monomerically-Reference-Cited by-同舟云学术

A low-angle laser light scattering study of the association behavior of a major membrane protein of Rhodospirillum rubrum chromatophore at various concentrations of sodium dodecyl sulfate where polypeptides derived from water-soluble globular proteins are solubilized monomerically

Published:1981-04 Issue:2 Volume:668 Page:290-298
ISSN:0005-2795
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure

Author:

Miyake Jun,Takagi Toshio

Publisher

Elsevier BV

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous)

Reference26 articles.

1. [1] Measurement of molecular weights by electrophoresis on SDS-acrylamide gel

2. High-Speed Gel Filtration of Polypeptides in Sodium Dodecyl Sulfate

3. Free-boundary Electrophoresis of Sodium Dodecyl Sulfate-Protein Polypeptide Complexes with Special Reference to SDS-Polyacrylamide Gel Electrophoresis

4. Proton Magnetic Resonance Studies of the Binding of an Anionic Surfactant with a Benzene Ring to a Protein Polypeptide with Special Reference to SDS-polyacrylamide Gel Electrophoresis

5. Binding Isotherms of Sodium Dodecyl Sulfate to Protein Polypeptides with Special Reference to SDS-polyacylamide Gel Electrophoresis

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