Subunit interactions in gamma-glutamyl transpeptidase. Reconstitution of the active species from isolated subunits.

This publication has 27 references indexed in Scilit:

• Interaction of the antitumor drug, L‐(αS, 5S)‐α‐amino‐3‐chloro‐4,5‐dihydro‐5‐isoxazoleacetic acid (AT‐125) with renal brush border membranes
  FEBS Letters, 1980
• Affinity labeling of γ‐glutamyl transpeptidase by glutamine antagonists
  FEBS Letters, 1980
• The inhibition of γ-glutamyl transpeptidase and glutathione metabolism of isolated rat kidney cells by L-(αS, 5S)-α-amino-3-chloro-4, 5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501)
  Biochemical and Biophysical Research Communications, 1980
• Latent Active Site in Rat-Kidney gamma-Glutamyl Transpeptidase. The Refolding Process of the Large Subunit and Characterization of the Renatured Enzyme
  European Journal of Biochemistry, 1980
• Ultrastructural localization of γ‐glutamyl transpeptidase in rat kidney and jejunum
  FEBS Letters, 1979
• Evidence for the presence of a latent active site in the large subunit of rat kidney γ-glutamyl transpeptidase
  Biochemical and Biophysical Research Communications, 1978
• Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit.
  Proceedings of the National Academy of Sciences, 1977
• Glutathione and Related γ-Glutamyl Compounds: Biosynthesis and Utilization
  Annual Review of Biochemistry, 1976
• gamma-Glutamyl Transpeptidase of Sheep-Kidney Cortex. Isolation, Catalytic Properties and Dissociation into Two Polypeptide Chains
  European Journal of Biochemistry, 1976
• On the Enzymology of Amino Acid Transport
  Science, 1973