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Plant Physiology 74:459-463 (1984)
© 1984 American Society of Plant Biologists

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Articles

Starch Degradation in Synchronously Grown Chlamydomonas reinhardtii and Characterization of the Amylase 1

Carolyn Levi2 and Martin Gibbs

Institute for Photobiology of Cells and Organelles, Brandeis University, Waltham, Massachusetts 02254

The activities of amylase and phosphorylase were monitored during the 12-hour light/dark synchronous cell cycle of autotrophically grown Chlamydomonas reinhardtii 11-32/90. The activity of amylase increased from 7.3 to 42 micromole reducing equivalents per 109 cells per hour while phosphorylase increased from 43 to 214 micromole glucose 1-phosphate released per 109 cells per hour between the midlight and middark periods. Cellular fractionation indicated that both enzymes were localized solely within the chloroplast. The pH optima for amylase and phosphorylase were 6.7 to 7.6 and 6.0 to 7.4, respectively. The amylase is a heat-labile {alpha}-amylase which is insensitive to ethylenetetraaecetate but inhibited by N-ethylmaleimide.

2 Present address: Department of Plant Pathology, University of Wisconsin—Madison, 1630 Linden Drive, Madison, WI 53706.

1 Supported by National Science Foundation PCM 79-22612.




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Copyright © 1984 by the American Society of Plant Biologists