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Yeast glyoxalase I. Circular dichroic spectra and pH effects

  • Kenneth T. Douglas*
  • , Andrew P. Seddon
  • , Yashushi Nakagawa
  • *Corresponding author for this work
  • The University of Essex
  • Michael Reese Hospital

Research output: Contribution to journal › Article › peer-review

Abstract

1. 1. Large scale isolation and physicochemical characterisation of yeast glyoxalase I showed that this enzyme contained small amounts of carbohydrates. 2. 2. Circular dichroic spectra of the enzyme measured in the presence and absence of S-(p-bromobenzyl)glutathione indicated perturbation of a tyrosine on binding of this competitive inhibitor. 3. 3. Values of Ki for competitive inhibitors were pH invariant over the accessible pH range.

Original languageEnglish
Pages (from-to)549-555
Number of pages7
JournalInternational journal of biochemistry
Volume18
Issue number6
DOIs
Publication statusPublished - 1986

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