Isolation and Purification of Protein Responsible for the Conversion of Dimethylallylpyrophosphate from Poplar Leaves into Isoprene

Isolation and Purification of Protein Responsible for the Conversion of... The protein converting dimethylallylpyrophosphate (DMAPP) into isoprene in vitrowas isolated and purified 3000-fold from leaves of berry-bearing poplar (Populus deltoidesMarsh.). As the enzyme was purified, its specific activity increased and at the final stage reached 266 nmol/(min mg protein). The enzyme was eluted by anion-exchange chromatography in a 120–170 mM NaCl gradient and by chromatography on the hydroxyapatite column in 170 mM sodium phosphate. The active molecular weight of the protein determined by gel filtration was 100–110 kD. As the enzyme was purified, the K Mvalue increased from 2 to 9 mM. A parallelism isoprene emission from DMAPP and an increase in the specific activity of the enzyme as it was purified proved that the enzyme catalyzed isoprene emission. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Isolation and Purification of Protein Responsible for the Conversion of Dimethylallylpyrophosphate from Poplar Leaves into Isoprene

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2001 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/A:1009008318764
Publisher site
See Article on Publisher Site

Abstract

The protein converting dimethylallylpyrophosphate (DMAPP) into isoprene in vitrowas isolated and purified 3000-fold from leaves of berry-bearing poplar (Populus deltoidesMarsh.). As the enzyme was purified, its specific activity increased and at the final stage reached 266 nmol/(min mg protein). The enzyme was eluted by anion-exchange chromatography in a 120–170 mM NaCl gradient and by chromatography on the hydroxyapatite column in 170 mM sodium phosphate. The active molecular weight of the protein determined by gel filtration was 100–110 kD. As the enzyme was purified, the K Mvalue increased from 2 to 9 mM. A parallelism isoprene emission from DMAPP and an increase in the specific activity of the enzyme as it was purified proved that the enzyme catalyzed isoprene emission.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Oct 10, 2004

References

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