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Plant and Cell Physiology, 1994, Vol. 35, No. 8 1179-1184
© 1994

Partial Purification and Immunocytocharacterization of the Plasma Membrane ATPase of Jerusalem artichoke (Helianthus tuberosus L.) Tubers in Relation to Dormancy

Franck Chaubron1,2, Fabien Robert1, Michel Gendraud1 and Gilles Pétel1,3

1Laboratoire de Physiologie Intégrée de I'Arbre Fruitier (P.I.A.F.), Unité Associée INRA-Université Blaise Pascal (Clermont II) 4, rue Ledru, 63038 Clermont-Ferrand Cedex 01, France
2Scottish Crop Research Institute (S.C.R.I.) Invergowrie, Dundee DD2 5DA, Scotland, U.K.

3To whom reprint requests should be sent.

Plasmalemma ATPase from Jerusalem artichoke tubers was studied in relation to the dormancy of tubers. After partial purification, one peptide of 110 kDa appeared on SDS PAGE electrophoresis from dormant and non-dormant materials. ATPase specific activity was twice higher on dormant material in the crude and solubilized fractions, but was the same in both materials after partial purification. Immunolabeling of this enzyme was made using a specific antibody raised against the C terminal portion of the H+-ATPase from Arabidopsis thaliana. Immunolabeling was more pronounced in dormant material, in vitro and in situ. Several works had shown that the C terminal part of the enzyme could be involved in its regulation. The results presented are discussed in relation to the hypothesis according to which an internal effector could modulated the plasmalemma ATPase activity, during dormancy breaking.

(Received October 25, 1993; Accepted September 6, 1994)
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