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Plant Physiology 93:785-790 (1990)
© 1990 American Society of Plant Biologists

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Metabolism and Enzymology

The Subunit Structure of Potato Tuber ADPglucose Pyrophosphorylase 1

Thomas W. Okita, Paul A. Nakata, Joseph M. Anderson, Joseph Sowokinos2, Matthew Morell3 and Jack Preiss

Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, Department of Horticulture, University of Minnesota, St. Paul, Minnesota 55108, Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824

ADPglucose pyrophosphorylase has been extensively purified from potato (Solanum tuberosum L.) tuber tissue to study its structure. By employing a modified published procedure (JR Sowokinos, J Preiss [1982] Plant Physiol 69: 1459-1466) together with Mono Q chromatography, a near homogeneous enzyme preparation was obtained with substantial improvement in enzyme yield and specific activity. In single dimensional sodium dodecyl sulfate polyacrylamide gels, the enzyme migrated as a single polypeptide band with a mobility of about 50,000 daltons. Analysis by two-dimensional polyacrylamide gel electrophoresis, however, revealed the presence of two types of subunits which could be distinguished by their slight differences in net charge and molecular weight. The smaller potato tuber subunit was recognized by antiserum prepared against the smaller spinach leaf 51 kilodalton ADPglucose pyrophosphorylase subunit. In contrast, the anti-54 kilodalton raised against the spinach leaf subunit did not significantly react to the tuber enzyme subunits. The results are consistent with the hypothesis that the potato tuber ADPglucose pyrophosphorylase is not composed of a simple homotetramer as previously suggested, but is a product of two separate and distinct subunits as observed for the spinach leaf and maize enzymes.

2 Present address: Red River Valley Potato Research Laboratory, Box 113, East Grand Forks, MN 56721.

3 Present address: Plant Environment Biology Group, Research School of Biological Science, Australian National University, Canberra, A.C.T. 2601, Australia.

1 Supported in part by grants from the U.S. Department of Energy (DE-FG06-87ER13699), the McKnight Foundation and Project 0590, College of Agriculture and Home Economics Research Center, Washington State University to T. W. O. and the National Science Foundation (DMB86-10319), the McKnight Foundation and the USDA/DOE/NSF Plant Science Program to J. P.




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