Journal Article

Purification and Some Properties of Pheophorbidase in <i>Chenopodium album</i>

Kenji Watanabe, Hiroyuki Ohta, Tohru Tsuchiya, Bunzo Mikami, Tatsuru Masuda, Yuzo Shioi and Ken-ichiro Takamiya

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 40, issue 1, pages 104-108
Published in print January 1999 | ISSN: 0032-0781
Published online January 1999 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/oxfordjournals.pcp.a029466
Purification and Some Properties of Pheophorbidase in Chenopodium album

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A novel enzyme, pheophorbidase, which catalyzes the conversion of pheophorbide a to C-132-carboxylpyropheophorbide a, was purified from Chenopodium album leaves. The purified enzyme showed two bands of 28 kDa and 29 kDa on SDS-PAGE. The molecular mass of the native pheophorbidase was 105 kDa. The N-terminal amino acid sequence for the 28-kDa protein could be determined, whereas the N-terminus of the 29-kDa protein was blocked. Immunochemical and enzyme activity analyses revealed that pheophorbidase is located in an extra-plastidic part of the cell.

Keywords: Chenopodium album; Chlorophyll degradation; Chlorophyllase (EC 3.1.1.14); Pheophorbidase; Pheophorbide a; Pyropheophorbide a

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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