Plant Physiol. Drug Metab Dispos
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Plant Physiology 85:87-90 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Partial Purification of Gibberellin Oxidases from Spinach Leaves 1

Sarah J. Gilmour2, Anthony B. Bleecker and Jan A. D. Zeevaart

MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824

Four enzyme activities catalyzing the following oxidative steps in the gibberellin (GA) biosynthetic pathway have been extracted from spinach (Spinacia oleracea L.) leaves after exposure to 8 long days: GA12 -> GA53 -> GA44 -> GA19 -> GA20. Two of these, GA53 oxidase and GA19 oxidase, were separable from the other two, GA44 oxidase and GA12 13-hydroxylase, by anion exchange high performance liquid chromatography (HPLC). Apparent molecular weights of the four enzymes as determined by gel filtration HPLC are: GA12 13-hydroxylase, 28,400; GA53 oxidase, 42,500; GA44 oxidase, 38,100; GA19 oxidase, 39,500. GA44 oxidase was purified approximately 100-fold in 0.3% yield by a combination of ammonium sulfate fractionation, anion exchange HPLC, phenyl-Sepharose chromatography and gel filtration HPLC.

2 Present address: Department of Crop and Soil Science, Michigan State University, East Lansing, MI 48824.

1 Supported by the National Science Foundation through grant No. PCM 83-04229 and by the United States Department of Energy under Contract No. DE-AC02-76ERO-1338.




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S. D. Jackson, P. E. James, E. Carrera, S. Prat, and B. Thomas
Regulation of Transcript Levels of a Potato Gibberellin 20-Oxidase Gene by Light and Phytochrome B
Plant Physiology, September 1, 2000; 124(1): 423 - 430.
[Abstract] [Full Text]


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Copyright © 1987 by the American Society of Plant Biologists