Microsomal polypeptides in sunflower (Helianthus annuus): Comparison between normal type before and after cold-induction, and a high oleic acid mutant [oleate desaturase, induction].
1994
Sarmiento C. | Mancha M. | Garces R.
Differences in high-resolution two-dimensional gel electrophoresis patterns of microsomal proteins from developing normal sunflower (Helianthus annuus L.) seeds before and after cold-induction, and also from normal and a high oleic sunflower mutant have been studied in order to detect the polypeptides associated with the microsomal Delta12-desaturase activity and its regulation by temperature. Proteins were obtained from developing seeds of two isogenic sunflower lines HA-89 (normal) and HA-OL9 (high oleic) which greatly differed in linoleic acid content and "in vitro" oleate desaturase activity. In the high oleic mutant, four polypeptides of about 32 kDa and two of 33 kDa were found to change in position, to the same extent, toward a lower isoelectric point in the high oleic mutant. Also, two polypeptides, of 32 and 49 kDa each, appeared in the mutant. Quantitative differences between cold-induced seeds (10 deg C, 24 h) and their non-induced controls were found. One polypeptide of 43 kDa decreased in the coldtreated seeds and two others, of 30 and 32 kDa each, increased markedly after cold induction. Some of these polypeptides could be related to oleate desaturase activity or its regulation by temperature.
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