Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus

A R Clarke, A D Waldman, I Munro, J J Holbrook

Research output: Contribution to journalArticlepeer-review

Abstract

Time-resolved measurements of the fluorescence anisotropy of an extrinsic dye-group attached to lactate dehydrogenase from B. stearothermophilus revealed that the rotational correlation time of the enzyme at low concentrations is 55 ns, while at high enzyme concentrations or in the presence of fructose 1,6-bisphosphate (Fru-1,6-P2) the correlation time increases to 95 ns. These correlation times are consistent with a change in Mr from 85 000 +/- 12 000 (dimer) to 150 000 +/- 22 000 (tetramer) and show that the tetrameric state can be induced either by raising the protein concentration or by the addition of the ligand. We have confirmed this change in molecular weight by gel-filtration experiments. In the ligand-induced tetramer, two Fru-1,6-P2 molecules are bound.

Original languageEnglish
Pages (from-to)375-9
Number of pages5
JournalBBA - Bioenergetics
Volume828
Issue number3
Publication statusPublished - 29 Apr 1985

Keywords

  • Binding Sites
  • Fluorescence Polarization
  • Fructosediphosphates
  • Geobacillus stearothermophilus
  • L-Lactate Dehydrogenase
  • Molecular Weight
  • Journal Article
  • Research Support, Non-U.S. Gov't

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