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. 1984 Mar;74(3):459–463. doi: 10.1104/pp.74.3.459

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

Carolyn Levi 1,2, Martin Gibbs 1
PMCID: PMC1066708  PMID: 16663444

Abstract

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 α-amylase which is insensitive to ethylenetetraaecetate but inhibited by N-ethylmaleimide.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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