The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain

Biochem J. 1970 Apr;117(2):341-6. doi: 10.1042/bj1170341.

Abstract

Stem bromelain that had been irreversibly inhibited with 1,3-dibromo[2-(14)C]-acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and alpha-chymotrypsin three radioactive peptides were isolated chromatographically. The amino acid sequences around the cross-linked cysteine and histidine residues were determined and showed a high degree of homology with those around the active-site cysteine and histidine residues of papain and ficin.

MeSH terms

  • Amino Acid Sequence
  • Bromelains / analysis*
  • Bromelains / antagonists & inhibitors
  • Carbon Isotopes
  • Chymotrypsin
  • Cysteine / analysis*
  • Histidine / analysis*
  • Iodoacetates / pharmacology
  • Papain / analysis
  • Peptide Hydrolases / analysis
  • Plants, Edible
  • Trypsin

Substances

  • Carbon Isotopes
  • Iodoacetates
  • Histidine
  • Bromelains
  • Peptide Hydrolases
  • Chymotrypsin
  • Trypsin
  • Papain
  • Cysteine