Glycerol as an agent eliciting small conformational changes in alcohol dehydrogenase.

Yeast alcohol dehydrogenase is an example of a protein in which the K-m for substrate is substantially decreased by the presence of glycerol. The polyol has the effect at pH 8.0 or above of decreasing K-m and K-s for substrate and of altering both the protein's intrinsic fluorescence and ultraviolet absorption difference spectrum. The relationship between each of thse parameters and glycerol concentration displays a transition at a glycerol concentration of 20%. Circular dichroism values for the enzyme are not affected by glycerol over a large range of concentration and temperature. Treatment of the enzyme with glutaraldehyde results in the formation of cross-linked tetramers, the K-m of which are not altered by the presence of the solvent. The data are interpreted as reflecting a change in the conformation of the protein induced by glycerol.

• Publication year

  1975

• Venue

  Journal of Biological Chemistry

• Publication date

  1975-05-25

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0021-9258(19)41467-1PMID 165183
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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