Plant Physiol. Drug Metab Dispos
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Plant Physiology 90:624-630 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Arginine Metabolism in Developing Soybean Cotyledons 1

I. Relationship to Nitrogen Nutrition

Barry J. Micallef and Barry J. Shelp

Department of Horticultural Science, University of Guelph, Guelph, Ontario NIG 2W1, Canada

The free and protein amino acid composition of Glycine max (L.) Merrill cotyledons was determined for the entire developmental period using high performance liquid chromatography. Arginine constituted 18% of the total protein nitrogen throughout development, and there was a linear arginine nitrogen accumulation rate of 1212 nanomoles per cotyledon per day between 16 and 58 days after anthesis. Arginine and asparagine were major constituents of the free amino acid pool, constituting 14 to 62% and 2 to 41% of the total free amino acid nitrogen, respectively. The urea cycle intermediates, citrulline, ornithine, and argininosuccinate were also detected in the free pool. A comparison of the amino acid composition of cotyledonary protein and of seedcoat exudate suggested that 72% of the cotyledon's arginine requirement is satisfied by in situ biosynthesis, and that 20% of the transformed nitrogen is incorporated into arginine. Also, [1-14C]glutamate and [U-14C]glutamine were fed to excised cotyledons. After 4 hours, 14C was incorporated into protein and released as 14CO2, but none was incorporated into the C-1 and C-6 positions of free and protein arginine, determined using arginine-specific enzyme-linked assays. It is not currently known whether arginine biosynthesis in the cotyledon involves glutamate delivered from the mother plant or glutamate derived in situ.


1 Supported by an operating grant to B. J. S. from the Natural Sciences and Engineering Research Council of Canada. B. J. M. was the recipient of an Ontario Graduate Scholarship.




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A. Goldraij, L. J. Beamer, and J. C. Polacco
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A. Goldraij and J. C. Polacco
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