89911-97-7Relevant articles and documents
A 37-kDa peroxidase secreted from liverworts in response to chemical stress
Hirata, Toshifumi,Ashida, Yoshiyuki,Mori, Hideyuki,Yoshinaga, Daisuke,Goad, Lionel J.
, p. 197 - 202 (2000)
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 pI of about 10 and an optimal pH of 6.5. The peroxidase was thermally stable at 50°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. (C) 2000 Elsevier Science Ltd.
Synthesis of bryophyte components. 3. New syntheses of Perrottetines E, F and G
Eicher,Walter
, p. 469 - 473 (2007/10/02)
Efficient and expeditious syntheses of the Perrottetines E, F and G (4',5-bis(m-hydroxyphenethyl)diphenyl ether derivatives) are developed, which give rise to these biologically active linear bis(bibenzyl) derivatives on a preparative scale.