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THE PLANT CELL, Vol 8, Issue 7 1121-1135, Copyright © 1996 by American Society of Plant Biologists
Identification of the Major Starch Synthase in the Soluble Fraction of Potato Tubers
J. Marshall, C. Sidebottom, M. Debet, C. Martin, A. M. Smith and A. Edwards
John Innes Centre, Colney Lane, Norwich NR4 7UH, United Kingdom
The major isoform of starch synthase from the soluble fraction of
developing potato tubers has been purified and used to prepare an antibody
and isolate a cDNA. The protein is 140 kD, and it is distinctly different
in predicted primary amino acid sequence from other isoforms of the enzyme
thus far described. Immunoinhibition and immunoblotting experiments and
analysis of tubers in which activity of the isoform was reduced through
expression of antisense mRNA revealed that the isoform accounts for ~80% of
the activity in the soluble fraction of the tuber and that it is also bound
to starch granules. Severe reductions in activity had no discernible effect
on starch content or amylose-to-amylopectin ratio of starch in tubers.
However, they caused a profound change in the morphology of starch
granules, indicative of important underlying changes in the structure of
starch polymers within the granule.
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