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Plant Physiology 63:468-473 (1979)
© 1979 American Society of Plant Biologists

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Articles

Isolation and Enzymic Characterization of Euglena Proplastids

Alex Dockerty and Michael J. Merrett

1 Postgraduate School of Studies in Biological Sciences, University of Bradford, Yorkshire BD7 1DP England

Organelles were isolated from dark-grown Euglena gracilis Klebs by sucrose density gradient centrifugation. Plastids, identified by triosephosphate isomerase and NADP glyoxylate reductase were present at an equilibrium density of 1.24 grams per cubic centimeter clearly separated from mitochondria at an equilibrium density of 1.22 grams per cubic centimeter. Assay for choline phosphotransferase and glucose-6-phosphatase showed that endoplasmic reticulum membranes were present at a density of 1.12 grams per cubic centimeter. The plastid fraction contained phosphofructokinase, pyruvate kinase, triosephosphate isomerase and aldolase indicating the operation of a glycolytic pathway. During regreening pyruvate kinase and phosphofructokinase in the developing proplastid decreased, neither enzyme being present in the mature chloroplast. However, plastids were present in the photosynthetic cell as shown by a peak of glycolysis enzymes at an equilibrium density of 1.24 grams per cubic centimeter.

The integrity of isolated plastids was demonstrated by their capacity for protein synthesis. Plastids isolated from dark-grown cells rapidly incorporated [35S]methionine into protein with an absolute dependence on added ATP. The large subunit of ribulose diphosphate carboxylase was the major polypeptide synthesized by these isolated plastids.




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C. Sulli and S. D. Schwartzbach
The Polyprotein Precursor to the Euglena Light-harvesting Chlorophyll a/b-binding Protein Is Transported to the Golgi Apparatus Prior to Chloroplast Import and Polyprotein Processing
J. Biol. Chem., June 2, 1995; 270(22): 13084 - 13090.
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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1979 by the American Society of Plant Biologists