Gel filtration, the chromatographic separation of proteins on columns of gel particles of various nature, has empirically been found to constitute a useful tool for molecular size determination (l-6), as indicated by a variety of applications. Few attempts have been made to utilize the interaction o
The determination of molecular weights of biologically active proteins by cetyltrimethylammonium bromide-polyacrylamide gel electrophoresis
โ Scribed by Dianne T. Akin; Raymond Shapira; Joseph M. Kinkade Jr.
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 925 KB
- Volume
- 145
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
A novel cetyltrimethylammonium bromide-polyacrylamide gel electrophoresis system which is useful for the separation of native forms of proteins consistent with their molecular weights is reported here. Many proteins examined in this system demonstrated the same association patterns which have been shown by other techniques to exist under nondenaturing conditions. In addition, biological activity could be assayed directly in the gel after electrophoresis. Based on the peculiar characteristics of cetyltrimethylammonium bromide, a possible explanation which may account for the behavior of proteins in this system is presented. o 1985 Academic Press. Inc.
๐ SIMILAR VOLUMES
A polyacrylamide gel elec&ophoresis system is described which employs the nonionic detergent T&on X-100 as a protein solvent. Aside from the obvious advantages of this detergent over ionic detergents and urea in the preservation of protein structure and function, it is demonstrated that the ancillar