Co-Authors:
Perl, M., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Swartzberg, D., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Izhar, S., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Abstract:
Soluble and membrane-bound fractions of plant leaves, cell suspension cultures and seedlings of petunia were examined for phosphohydrolase activity on p-nitrophenyl phosphate (pNPPase) and adenosine triphosphate (ATPase). One cytoplasmic male-sterile (CMS) and one fertile (F) line was examined for each tissue. Both pNPPase and ATPase exhibited a broad optimal activity between pH 5.5-7.0 for the membrane-bound fraction and between 4.5-7.0 for the soluble fractions. The activity of both were inhibited by divalent ions including Mg2+. At pH 7.2, the activities on various triphosphonucleotides were similar and they were hydrolyzed by a rate of 20-50% of that of ATP. Significant differences between CMS and F extracts were: (a) higher activities in CMS membranes; (b) lower Ea (energy of activation) values for activities in CMS membrane functions; (c) seedling and cell-culture CMS extracts exhibited a higher sensitivity to high temperature denaturation; (d) the hydrolase activity on monoand triphospho-cytosine compounds was significantly higher in CMS than in F membranes. © 1993 Springer-Verlag.
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