Abstract
The supramolecular structure of oligomeric enzymes can be specifically regulated by changing the size of an inner cavity of Aerosol OT reversed micelles in octane. Both D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and lactate dehydrogenase (LDH) reveal an ability to exist and function in monomeric, dimeric and tetrameric forms (homooligomers). Various heterooligomeric complexes, in particular, GAPDH monomer--LDH monomer, GAPDH dimer--LDH tetramer were detected in reversed micelles.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Catalysis
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Dioctyl Sulfosuccinic Acid
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Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry*
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Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
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L-Lactate Dehydrogenase / chemistry*
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L-Lactate Dehydrogenase / metabolism
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Macromolecular Substances
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Micelles*
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Octanes
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Polymers
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Protein Conformation
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Rabbits
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Solvents
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Surface-Active Agents
Substances
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Macromolecular Substances
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Micelles
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Octanes
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Peptide Fragments
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Polymers
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Solvents
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Surface-Active Agents
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Dioctyl Sulfosuccinic Acid
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glyceraldehyde 3-phosphate dehydrogenase (304-313)
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L-Lactate Dehydrogenase
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Glyceraldehyde-3-Phosphate Dehydrogenases
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octane