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Plant and Cell Physiology, 1997, Vol. 38, No. 9 1026-1031
© 1997

Purification and Characterization of Two Isozymes of Chlorophyllase from Mature Leaves of Chenopodium album

Tohru Tsuchiya1, Hiroyuki Ohta1, Tatsuru Masuda1, Bunzo Mikami2, Noriaki Kita1, Yuzo Shioi1,3 and Ken-ichiro Takamiya1,4

1 Tokyo Institute of Technology, Department of Biological Sciences, Faculty of Bioscience and Biotechnology Nagatsuta, Midori-ku, Yokohama, 226 Japan
2 Research Institute for Food Science, Kyoto University Uji, Kyoto, 611 Japan

4Corresponding author

Chlorophyllase (Chlase) was purified from mature leaves of Chenopodium album, and its enzymatic properties were investigated. Chlase was extracted from acetone powder of C. album and purified by the following chroma-tographic procedures: hydrophobic chromatography, Con A Sepharose, Heparin affinity chromatography, Mono Q ion-exchange chromatography, and gel-filtration. Con A Sepharose affinity chromatography and gel-filtration were the most effective steps on the purification. On Mono Q chromatography, the Chlase preparation separated into two major and one minor fractions that exhibited Chlase activity. The two major Chlases were purified to homogeneity. Their molecular masses were estimated as 41.3 kDa and 40.2 kDa by SDS-PAGE. The optimum pH and Km values of these two Chlases were similar. Their N-terminal amino acid sequences were almost identical except for a deletion in the tenth amino acid residue in one of the Chlase; there was no homologous protein detected by database search.

3Present address: Department of Biology and Geoscience, Faculty of Science, Shizuoka University, 836 Ohya, Shizuoka, 422 Japan.

(Received January 10, 1997; Accepted June 27, 1997)
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