Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 72:474-480 (1983)
© 1983 American Society of Plant Biologists

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Articles

Changes in Starch Formation and Activities of Sucrose Phosphate Synthase and Cytoplasmic Fructose-1,6-bisphosphatase in Response to Source-Sink Alterations 1

Thomas W. Rufty, Jr. and Steven C. Huber

United States Department of Agriculture, Agriculture Research Service, North Carolina State University, Raleigh, North Carolina 27650, Department of Crop Science, North Carolina State University, Raleigh, North Carolina 27650, Department of Botany, North Carolina State University, Raleigh, North Carolina 27650

Short term experiments were conducted with vegetative soybean plants (Glycine max L. Merr. `Ransom' or `Arksoy') to determine whether sourcesink manipulations, which rapidly changed the `demand' for sucrose and partitioning of photosynthetically fixed carbon into starch, were associated with alterations in activities of sucrose-P synthase and/or cytoplasmic fructose-1,6-bisphosphatase in leaf extracts. When demand for sucrose from a particular source leaf was increased by defoliation of other source leaves, starch accumulation was restricted and activities of both enzymes were markedly enhanced. When demand for sucrose from source leaves was limited by excision, starch accumulation in the detached leaves was increased while activity of sucrose-P synthase declined sharply. The consistent responsiveness of sucrose-P synthase activity to changes in demand for sucrose supports the contention that regulation of sucrose-P synthase is an integral component of the system which controls sucrose biosynthesis and partitioning of carbon between starch and sucrose biosynthesis in the light.


1 Cooperative investigations of the United States Department of Agriculture, Agricultural Research Service, and North Carolina Agricultural Research Service, Raleigh, NC. This is Paper 8613 of the Journal Series of the North Carolina Agricultural Research Service, Raleigh, NC 27650.




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