Enzyme conformational alterations detected by partition column chromatography

Christer Wingren, Ulla-Britt Hansson

Research output: Contribution to journalArticlepeer-review

Abstract

In this paper, we demonstrate the ability of liquid-liquid partition chromatography (LLPC) to detect conformational alterations occurring in well-characterized enzymes. The conformational changes induced in dehydrogenases such as alcohol dehydrogenase (ADH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), lactate dehydrogenases (LDH) and malate dehydrogenase (MDH) upon binding of ligand(s) were detectable by LLPC. The ligand-dependent equilibrium between two forms of citrate synthase (CS), glutamate-oxaloacetate transaminase (GOT), hexokinase (HK) and 3-phosphoglycerate kinase (PGK) could also be demonstrated. Furthermore, different conformational forms of some of the apoenzymes could also be detected and separated by LLPC. The results obtained here are discussed in relation to those obtained by other methods.
Original languageEnglish
Pages (from-to)113-122
JournalJournal of Chromatography. B
Volume680
Issue number1-2
DOIs
Publication statusPublished - 1996

Subject classification (UKÄ)

  • Biological Sciences

Free keywords

  • Partition column chromatography
  • Conformational changes
  • Enzymes

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