A 37-kDa peroxidase secreted from liverworts in response to chemical stress.
A peroxidase was purified from the culture medium of a suspension culture of Marchantia polymorpha (liverwort) after treatment with bornyl acetate, which acts as a chemical stress agent to the cells. The peroxidase was characterised as a glycoprotein of molecular mass 37-kDa having a pl of about 10 and an optimal pH of 6.5. The peroxidase was thermally stable at 50 degrees C for up to 60 min. The partial amino acid sequence of the peroxidase was determined and found to be dissimilar to the amino acid sequences of other higher plant peroxidases. The oxidative polymerization of lunularin by this peroxidase was examined and the formation of a dimer, a trimer and a tetramer was demonstrated by negative ion Fast Atom Bombardment (FAB)-mass spectroscopy of the reaction products.
Hirata
T
T
Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima, Japan. thirata@sci.hiroshima-u.ac.jp
Ashida
Y
Y
Mori
H
H
Yoshinaga
D
D
Goad
L J
LJ
D001632:Bibenzyls; D001892:Camphanes / Q000494:pharmacology*; D002478:Cells, Cultured; D004795:Enzyme Stability; D008970:Molecular Weight; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000302:isolation & purification* / Q000378:metabolism; D010636:Phenols / Q000378:metabolism; D010944:Plants; D010946:Plants, Medicinal / Q000166:cytology / Q000201:enzymology*; D013267:Stilbenes
D001632:Bibenzyls; D001892:Camphanes; D010636:Phenols; D013267:Stilbenes; C071528:bornyl acetate; C121619:lunularin; D009195:Peroxidase