Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 85:182-187 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Subunit Structure of Spinach Leaf ADPglucose Pyrophosphorylase 1

Matthew K. Morell, Mark Bloom, Vicki Knowles2 and Jack Preiss

Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824-1319

To initiate structural studies of the ADPglucose pyrophosphorylase from spinach an improved purification procedure was devised. The modified purification scheme allowed the isolation of 20 to 30 milligrams pure enzyme from 10 kilogram of spinach leaves. Electrophoresis of the purified enzyme confirmed an earlier study which showed that the enzyme was putatively composed of two subunits (Copeland L, J Preiss 1981 Plant Physiol 68: 996-1001). The two subunits migrate as 51 and 54 kilodalton proteins upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both proteins can be detected on Western blots of leaf homogenates prepared under denaturing conditions suggesting that both subunits exist in vivo. Anion-exchange chromatography in the presence of urea allowed resolution of the 51 and 54 kilodalton proteins. They possess different N-terminal amino acid sequences and tryptic peptide maps. Western blot analysis reveals that the 51 and 54 kilodalton proteins are antigenically dissimilar. The 51 but not the 54 kilodalton protein is immunologically related to the ADPglucose pyrophosphorylase from maize endosperm and potato tuber.

2 Current address: Department of Biology, Queen's University, Kingston, Ontario, Canada K7L 3N6.

1 Supported in part by National Science Foundation research grants DMB 85-10088 and DMB 86-10319 and United States Public Health Service research grant AI22835.




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