May 10, 1979

Synthesis of active site-directed organometallic irreversible protease inhibitors

Biochimica Et Biophysica Acta
S WyrickC B Chae


p-Antimonybenzenesulfonyl fluoride and p-mercurybenzenesulfonyl fluoride irreversibly inhibit chymotrypsin (EC, trypsin (EC, and chromosomal protease, and these inhibitors appear to be as active as phenylmethanesulfonyl fluoride. The pretreatment of the proteases interferes with the phosphorylation of the active-site serine by diisopropylfluorophosphate suggesting that the organometallic inhibitors may also interact with the active site serine. The organometallic inhibitors may be used for localization of proteases in different parts of the cell by electron microscopy and p-mercurybenzenesulfonyl fluoride could also be used for isolation of proteases by sulfhydryl affinity chromatography.

  • References5
  • Citations4


Mentioned in this Paper

Establishment and Maintenance of Localization
Protease Inhibitors [MoA]
Trypsin Inhibitors
Cathepsin G
4-antimonybenzenesulfonyl fluoride
Peptide Hydrolases
Protein Phosphorylation
4-mercurybenzenesulfonyl fluoride

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