Literature DB >> 4003759

The determination of molecular weights of biologically active proteins by cetyltrimethylammonium bromide-polyacrylamide gel electrophoresis.

D T Akin, R Shapira, J M Kinkade.   

Abstract

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.

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Year:  1985        PMID: 4003759     DOI: 10.1016/0003-2697(85)90343-4

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  4 in total

1.  Purification and characterization of G proteins from human brain: modification of GTPase activity upon phosphorylation.

Authors:  C Sauvage; J F Rumigny; M Maitre
Journal:  Mol Cell Biochem       Date:  1991-09-18       Impact factor: 3.396

2.  Size separation of proteins by capillary zone electrophoresis with cationic hitchhiking.

Authors:  Vladislav Dolnik; William A Gurske
Journal:  Electrophoresis       Date:  2011-09-22       Impact factor: 3.535

3.  Separation of proteins using cetyltrimethylammonium bromide discontinuous gel electrophoresis.

Authors:  R E Akins; R S Tuan
Journal:  Mol Biotechnol       Date:  1994-06       Impact factor: 2.695

4.  Solubilization of growth hormone and other recombinant proteins from Escherichia coli inclusion bodies by using a cationic surfactant.

Authors:  N K Puri; E Crivelli; M Cardamone; R Fiddes; J Bertolini; B Ninham; M R Brandon
Journal:  Biochem J       Date:  1992-08-01       Impact factor: 3.857

  4 in total

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