Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 95:1214-1218 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Soybean Leaves Contain Multiple Lipoxygenases 1

W. Scott Grayburn, G. Russell Schneider, Thomas R. Hamilton-Kemp, Gerhard Bookjans, Kadum Ali and David F. Hildebrand

Department of Agronomy, University of Kentucky, Lexington, Kentucky 40546, Department of Horticulture, University of Kentucky, Lexington, Kentucky 40546

Chromatofocusing of soybean (Glycine max L.) leaf lipoxygenases revealed three distinct peaks of activity. Based on their isoelectric points (pls), pH optima, and mutant analysis it appears that the leaf isozymes are different from those described from mature soybean seed. At least one leaf lipoxygenase appears to differ from those found in hypocotyls. The pls of the main bands of the three leaf lipoxygenase peaks are 6.67, 5.91, and 5.67. The pH optima curves of three active fractions exhibit peaks at pH 6.2, 5.5, and 8.5, respectively. One of the fractions has two polypeptides with slightly different molecular weights, both of which react to soybean seed lipoxygenase antibodies. The other two fractions contain a polypeptide of unit molecular weight reacting with the lipoxygenase antibodies.


1 The investigation reported in this paper (No. 89-10-41) is in connection with a project of the Kentucky Agricultural Experiment Station and is published with approval of the Director.




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L. C. Stephenson, T. W. Bunker, W. E. Dubbs, and H. D. Grimes
Specific Soybean Lipoxygenases Localize to Discrete Subcellular Compartments and Their mRNAs Are Differentially Regulated by Source-Sink Status
Plant Physiology, March 1, 1998; 116(3): 923 - 933.
[Abstract] [Full Text]




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Copyright © 1991 by the American Society of Plant Biologists