Conversion of glutathione to glutathione disulfide, a catalytic function of gamma-glutamyl transpeptidase. Academic Article uri icon

Overview

MeSH Major

  • Glutathione
  • gamma-Glutamyltransferase

abstract

  • A purification procedure, based on that previously used for rat kidney gamma-glutamyl transpeptidase, was used for the purification of glutathione oxidase (which converts glutathione to gluthathione disulfide). The two activities co-purified, the ratio of the activities remaining constant through all steps of the isolation procedure. The purified enzyme was separable into 12 isozymic species by isoelectric focusing. All 12 isozymes exhibited a constant ratio of transpeptidase to glutathione oxidase activities, strongly supporting the conclusion that conversion of glutathione to glutathione disulfide is a catalytic function of gamma-glutamyl transpeptidase. Modulation of oxidase activity by inhibitors and acceptor substrates of transpeptidase is discussed in relation to the possible glutathione binding sites involved in gamma-glutamyl transfer and oxidase activities of the enzyme.

publication date

  • July 10, 1979

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 36385

Additional Document Info

start page

  • 5573

end page

  • 5

volume

  • 254

number

  • 13