The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain.
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.
D000595:Amino Acid Sequence; D001963:Bromelains / Q000032:analysis* / Q000037:antagonists & inhibitors; D002247:Carbon Isotopes; D002918:Chymotrypsin; D003545:Cysteine / Q000032:analysis*; D006639:Histidine / Q000032:analysis*; D007461:Iodoacetates / Q000494:pharmacology; D010206:Papain / Q000032:analysis; D010447:Peptide Hydrolases / Q000032:analysis; D010945:Plants, Edible; D014357:Trypsin
D002247:Carbon Isotopes; D007461:Iodoacetates; D006639:Histidine; D001963:Bromelains; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain; D003545:Cysteine