Phenyl-Sepharose chromatography of membrane proteins solubilized in Triton X-100

Steven D Carson, William H. Konigsberg

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Chromatography on phenyl-Sepharose provides a convenient means of concentrating "membrane" proteins, which bind Triton X-100, and of separating them from "soluble" proteins, which do not bind the detergent. As an example, chromatography on phenyl-Sepharose has been used in the purification of tissue factor from human brain and placenta. Triton X-100 extracts of brain and placenta are separated into two distinct protein fractions when chromatographed on phenyl-Sepharose. One fraction elutes in detergent-free buffer, whereas the other elutes only after saturation of the column with Triton X-100. The absence of proteins in fractions eluted prior to detergent saturation of the column suggested that, in the presence of Triton X-100, protein binding to phenyl-Sepharose occurred as a complex with the detergent. A propylene glycol concentration gradient eluted bound proteins and Triton X-100 over the same concentrations of propylene glycol.

Original languageEnglish (US)
Pages (from-to)398-401
Number of pages4
JournalAnalytical Biochemistry
Volume116
Issue number2
DOIs
StatePublished - Sep 15 1981

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Agarose Chromatography
Octoxynol
Chromatography
Membrane Proteins
Detergents
Propylene Glycol
Placenta
Brain
Proteins
Thromboplastin
Protein Binding
Purification
Buffers
phenyl-sepharose

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phenyl-Sepharose chromatography of membrane proteins solubilized in Triton X-100. / Carson, Steven D; Konigsberg, William H.

In: Analytical Biochemistry, Vol. 116, No. 2, 15.09.1981, p. 398-401.

Research output: Contribution to journalArticle

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