Capillary sodium dodecyl sulfate gel electrophoresis of proteins

A. Guttman, Judith A. Nolan, Nelson Cooke

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

In recent years, there has been considerable activity in the separation and characterization of protein molecules by sodium dodecylsulfate (SDS) gel electrophoresis with particular interest in using this technique to separate on the basis of size and to estimate molecular mass. In this paper we report a new improved and automated electrophoretic method in the form of high-performance capillary SDS gel electrophoresis. Rapid separations of protein molecules in the molecular mass range of 20 000-200 000 daltons were demonstrated with excellent linearity and intra- and inter-day reproducibility of the migration time. Monomer-dimer forms of the recombinant human ciliary neurotrophic factor were examined by the use of this method under reducing and non-reducing conditions.

Original languageEnglish
Pages (from-to)171-175
Number of pages5
JournalJournal of Chromatography A
Volume632
Issue number1-2
DOIs
Publication statusPublished - Feb 19 1993

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Molecular mass
Electrophoresis
Sodium Dodecyl Sulfate
Gels
Sodium
Molecules
Dimers
Proteins
Monomers
axokine

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry
  • Molecular Medicine

Cite this

Capillary sodium dodecyl sulfate gel electrophoresis of proteins. / Guttman, A.; Nolan, Judith A.; Cooke, Nelson.

In: Journal of Chromatography A, Vol. 632, No. 1-2, 19.02.1993, p. 171-175.

Research output: Contribution to journalArticle

Guttman, A. ; Nolan, Judith A. ; Cooke, Nelson. / Capillary sodium dodecyl sulfate gel electrophoresis of proteins. In: Journal of Chromatography A. 1993 ; Vol. 632, No. 1-2. pp. 171-175.
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