Purification and Some Properties of Pheophorbidase in Chenopodium album.

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. [ABSTRACT FROM AUTHOR]