Separation of glutathione transferase subunits from Proteus vulgaris by two-dimensional gel electrophoresis

Giaming Hong, Yi-Chih Chien, Cheng I. Chien

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Cytosolic glutathione transferases of Proteus vulgaris were purified by affinity chromatography and characterized by two-dimensional gel electrophoresis. Four different subunits were identified, and each subunit contained a different molecular mass, ranging from 26.2 kDa to 28.5 kDa; a different pI value, ranging from 8.2 to 9.4; and a different amount of protein fraction, ranging from 10% to 56%. All four subunits existed as basic proteins (pI > 7.0). From these results, we concluded that multiple forms of glutathione transferase enzymes existed in Proteus vulgaris, and four different glutathione transferase subunits were separated by 2-D gel electrophoresis.

Original languageEnglish
Pages (from-to)352-354
Number of pages3
JournalCurrent Microbiology
Volume47
Issue number4
DOIs
Publication statusPublished - 2003 Oct 1

Fingerprint

Proteus vulgaris
Electrophoresis, Gel, Two-Dimensional
Glutathione Transferase
Affinity Chromatography
Proteins
Enzymes

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

Cite this

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Separation of glutathione transferase subunits from Proteus vulgaris by two-dimensional gel electrophoresis. / Hong, Giaming; Chien, Yi-Chih; Chien, Cheng I.

In: Current Microbiology, Vol. 47, No. 4, 01.10.2003, p. 352-354.

Research output: Contribution to journalArticle

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