Abstract
A novel enzyme, pheophorbidase, which catalyzes the conversion of pheophorbide a to C-132-carboxylpyropheo-phorbide 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.
Author supplied keywords
Cite
CITATION STYLE
Watanabe, K., Ohta, H., Tsuchiya, T., Mikami, B., Masuda, T., Shioi, Y., & Takamiya, K. I. (1999). Purification and some properties of pheophorbidase in Chenopodium album. Plant and Cell Physiology, 40(1), 104–108. https://doi.org/10.1093/oxfordjournals.pcp.a029466
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.
