The aim of the work described in this paper was to characterize the tu
bers of potato (Solanum tuberosum var. Prairie) plants that had been t
ransformed with the Escherichia call ADPglucose pyrophosphorylase (EC
2.7.7.27) gene, glgC-16, under the control of a patatin promoter. Over
30 lines of transformed plants with increased ADPglucose pyrophosphor
ylase activity were obtained. The tubers of six of these lines were co
mpared with those of control plants expressing the gene for beta-glucu
ronidase. The average increase in pyrophosphorylase activity was 200%,
and the highest was 400%. Western immunoblotting of tuber extracts sh
owed that the amounts of glgC-16 protein were linearly related to the
extractable activity of the ADPglucose pyrophosphorylase. Cell fractio
nation studies showed that the increased activity of the pyrophosphory
lase in the glgC-16 tubers had a similar intracellular location, the a
myloplast fraction, to that found in the control tubers. No pleiotropi
c changes in the maximum catalytic activities of the following enzymes
could be detected in the glgC-16 tubers: sucrose synthase, fructokina
se, UDPglucose pyrophosphorylase, phosphofructokinase, soluble starch
synthase, starch branching enzyme, phosphoglucomutase and alkaline ino
rganic pyrophosphatase. The glgC-16 tubers are held to be suitable for
the study of the role of ADPglucose pyrophosphorylase in the control
of starch synthesis.