Use of trinitrobenzensulfonate for affinity labeling of lysine residues at phosphate binding sites of some enzymes

Arch Biochem Biophys. 1993 Apr;302(1):218-21. doi: 10.1006/abbi.1993.1202.

Abstract

Trinitrobenzensulfonate, a reagent for lysine residues, inactivates lamb liver 6-phosphogluconate dehydrogenase through affinity labeling. Complete inactivation is due to the binding of only one residue of reagent per enzyme subunit. Other enzymes with a phosphate binding site are also inactivated by affinity labeling. It appears that trinitrobenzensulfonate, when used at low concentrations, first binds to a phosphate binding site, then reacts with a nearby lysine residue. This reagent presents some advantages over pyridoxal phosphate, which has similar characteristics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Affinity Labels*
  • Animals
  • Binding Sites
  • Kinetics
  • Liver / enzymology
  • Lysine*
  • Phosphates / metabolism*
  • Phosphogluconate Dehydrogenase / antagonists & inhibitors
  • Phosphogluconate Dehydrogenase / chemistry
  • Sheep
  • Spectrophotometry
  • Trinitrobenzenesulfonic Acid / pharmacology*

Substances

  • Affinity Labels
  • Phosphates
  • Trinitrobenzenesulfonic Acid
  • Phosphogluconate Dehydrogenase
  • Lysine