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 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.
Hirata, Toshifumi,Ashida, Yoshiyuki,Mori, Hideyuki,Yoshinaga, Daisuke,Goad, Lionel J.
Total synthesis of polymorphatin A, a macrocyclic bisbibenzyl with boat configured arenes
Polymorphatin A was reported as a constituent of Marchantia polymorpha in 2007 following much speculation as to its likely existence as a natural product. Interest was rekindled when a claimed total synthesis revealed inconsistencies in spectral data betw
Almalki, Faisal A.,Sun, Wei,Light, Mark E.,Harrowven, David C.
(2020/09/04)
Synthesis of bryophyte components. 3. New syntheses of Perrottetines E, F and G
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.
Eicher,Walter
p. 469 - 473
(2007/10/02)
Perrottetins E, F, and G from Radula perrottetii (liverwort). Isolation, structure determination, and synthesis of perrottetin E
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Toyota,Tori,Takikawa,et al.
p. 6097 - 6100
(2007/10/02)
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