Purification and properties of N-formylmethionine aminopeptidase from rat liver

Biochim Biophys Acta. 1980 Nov 6;616(1):60-7. doi: 10.1016/0005-2744(80)90263-6.


A specific enzyme for the liberation of N-terminal N-formylmethionine from N-formylmethionyl peptides was purified 4750-fold from rat liver by successive applications of (NH4)SO4 precipitation, DEAE-cellulose, N-formylbestatin-AH-Sepharose 4B and AH-Sepharose 4B chromatography followed by Sepharose CL-6B gel filtration. The molecular weight was determined by gel filtration on Sepharose CL-6B as 290 000 +/- 5000. This was suggested to be a tetramer consisting of a subunit which was shown by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis to have a 72 000 +/- 2000 molecular weight. The optimum pH of the enzyme was 7.8. Cd2+ and Hg2+ were highly toxic to the enzyme. Michaelis constants of N-formylmethionyl leucine and N-formylmethionine beta-naphthylamide were 0.03 and 0.2 mM, respectively.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aminopeptidases / isolation & purification*
  • Animals
  • Chromatography, Affinity
  • Kinetics
  • Liver / enzymology*
  • Male
  • Molecular Weight
  • Rats


  • Aminopeptidases
  • N-formylmethionine aminopeptidase