Proteins in Denaturing Solvents: Gel Exclusion Studies
- 30 August 1968
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 161 (3844) , 906-907
- https://doi.org/10.1126/science.161.3844.906
Abstract
Many proteins are fully denatured and separated into component polypeptide chains in 6M guanidine hydrochloride containing mercaptoethanol and a chelating agent. In this and similar denaturing solvents, polypeptide chains of molecular weights from 2,000 to 100,000 can be eluted from 6 percent agarose columns and separated according to molecular weight. By this procedure molecular weights may be assigned to proteins (including many normally insoluble in nondenaturing solvents) without the uncertainties that arise when native molecules of unknown shape are studied.Keywords
This publication has 3 references indexed in Scilit:
- Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochlorideBiochemistry, 1968
- Proteins as Random Coils. I. Intrinsic Viscosities and Sedimentation Coefficients in Concentrated Guanidine HydrochlorideJournal of the American Chemical Society, 1967
- The Use of Cyanate for the Determination of NH2-terminal Residues in ProteinsJournal of Biological Chemistry, 1963