Journal Article

Purification and Characterization of Two Isozymes of Chlorophyllase from Mature Leaves of <i>Chenopodium album</i>

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

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 9, pages 1026-1031
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029267
Purification and Characterization of Two Isozymes of Chlorophyllase from Mature Leaves of Chenopodium album

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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.

Keywords: Chenopodium album; Chlorophyll; Chlorophyllase (EC 3.1.1.14); Chlorophyll degradation; Isozymes

Journal Article.  0 words. 

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

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