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Plant and Cell Physiology, 2001, Vol. 42, No. 4 433-440
© 2001 Oxford University Press

Characterization of Ascorbate Peroxidases from Unicellular Red Alga Galdieria partita

Satoshi Sano ,1,5, Masami Ueda1,2,3, Sakihito Kitajima1, Toru Takeda3, Shigeru Shigeoka3, Norihide Kurano4, Shigetoh Miyachi4, Chikahiro Miyake2 and Akiho Yokota ,1,2,6

1 Research Institute of Innovative Technology for the Earth, Kizu, Kyoto, 619-0292 Japan 2 Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, 630-0101 Japan 3 Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nakamachi, Nara, 631-8505 Japan 4 Kamaishi Laboratory, Marine Biotechnology Institute, Kamaishi, Iwate, 026-0001 Japan

Galdieria partita, a unicellular red alga isolated from acidic hot springs and tolerant to sulfur dioxide, has at least two ascorbate peroxidase (APX) isozymes. This was the first report to demonstrate that two isozymes of APX are found in algal cells. Two isozymes were separated from each other at the hydrophobic chromatography step of purification and named APX-A and APX-B after the elution order in the chromatography. APX-B accounted for 85% of the total activity. Both isozymes were purified. APXs from Galdieria were monomers whose molecular weights were about 28,000, similar to stromal APX of higher plants. APX-A cross-reacted with monoclonal antibody raised against APX of Euglena gracilis in immunoblotting, but APX-B did not, although the antibody can recognize all other APXs tested. The amino-terminal sequences of APX-A and -B from Galdieria had some homology with each other but little homology with those from other sources. Their Km values for ascorbate and hydrogen peroxide were comparable with those of APX from higher plants. Unlike the green algal enzymes, the donor specificities of Galdieria APXs were as high as those of plant chloroplastic APX. On the contrary, these APXs reduced tertiary-butyl hydroperoxide as an electron acceptor as APXs from Euglena and freshwater Chlamydomonas do. The inhibition of APX-A and -B by cyanide and azide, and characteristics of their light absorbance spectra indicated that they were heme peroxidases.

5 Present address: Department of Biological Resource Science, Faculty of Agriculture, Kyoto Prefectural University, Kyoto, 606-8522 Japan.

6 Corresponding author: E-mail, yokota@bs.aist-nara.ac.jp; Fax, +81-743-72-5569.


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