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This article in CS

  1. Vol. 38 No. 5, p. 1183-1189
    Received: Jan 8, 1998

    * Corresponding author(s): castonguayy@em.agr.ca
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Enzymatic Control of Soluble Carbohydrate Accumulation in Cold-Acclimated Crowns of Alfalfa

  1. Yves Castonguay  and
  2. Paul Nadeau
  1. Soil and Crop Research and Development Centre, Agriculture and Agri-Food Canada, 2560 Hochelaga Blvd., Sainte-Foy, Québec, Canada, G1V 2J3



Sucrose and the raffinose family of oligosaccharides (RFO), stachyose and raffinose, accumulate in crowns of alfalfa (Medicago sativa L.) during low temperature acclimation. In vitro and in vivo evidence from the literature suggests that these sugars might have important adaptive roles in freezing tolerance. To better understand the regulation of cold-induced accumulation of soluble sugars, we measured the activity of key regulatory enzymes involved in the metabolism of sucrose and RFO in crowns of three alfalfa cultivars of contrasting winterhardiness which had been acclimated to winter conditions. Both sucrose-phosphate synthase (SPS) and galactinol synthase (GS) showed markedly higher activity at low temperature. There was a close relationship between the activities of SPS and GS and the levels of sucrose and RFO, respectively. A delay of approximately 2 wk was observed between the rise in GS activity and RFO accumulation. For both SPS and GS, the increase in activity occurred earlier and reached higher levels in two winter hardy cultivars than in a nonhardy cultivar. In contrast, the activity of the RFO degrading enzyme alpha-galactosidase (α-gal) was identical in all cultivars. The activity of sucrose synthase (SS), mainly involved in sucrose hydrolysis, decreased during fall acclimation. In cold-acclimated alfalfa, both acid and neutral invertase activities were low and comparable in all cultivars. Our results indicate that differential accumulation of soluble sugars between alfalfa cultivars of contrasting winterhardiness is the result of differences in synthetic capacity rather than differences in hydrolytic activities.

Contribution No. 573 of the Sainte-Foy Research Centre.

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