Electrophoretic patterns of soluble protein fractions from cold-tolerant winter wheats (Triticum aestivum L. cv. Frederick and cv. Norstar) and cold-sensitive spring wheat (T. aestiaum L. cv. Glenlea) were analysed in hardened and unhardened plants. One and two-dimensional gel electrophoresis analysis reveals that cold hardening conditions induce changes in the soluble protein patterns. The most important is the accumulation of a high molecular weight protein in the range of 200 kDa. This protein accumulated at higher concentration in cold-tolerant cultivars compared to the coldsensitive one suggesting a correlation between the degree of freezing tolerance and the accumulation of this specific protein. In addition, the intensity of three protein bands (mol wt 48, 47 and 42 kDa) increased while that of five others (mol wt 93, 89, 80, 67 and 63 kDa) decreased during hardening. These changes occured in the three cultivars suggesting that they are part of the metabolic adjustments in response to low temperature rather than a specific change associated with the development of cold hardiness.
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Sarhan et al. (1987) studied this question.