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Microsomal polypeptides in sunflower ( Helianthus annum ). Comparison between normal type before and after cold‐induction, and a high oleic acid mutant
Author(s) -
Sarmiento Cristina,
Mancha Manuel,
Garcés Rafael
Publication year - 1994
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1994.tb00664.x
Subject(s) - helianthus annuus , sunflower , mutant , oleic acid , isoelectric point , biochemistry , biology , isoelectric focusing , microsome , gel electrophoresis , linoleic acid , in vitro , enzyme , horticulture , fatty acid , gene
Differences in high‐resolution two‐dimensional gel electrophoresis patterns of micro‐somal 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 Δ l2 ‐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°C, 24 h) and their non‐induced controls were found. One polypeptide of 43 kDa decreased in the cold‐treated seeds and two others, of 30 and 32 kDa each, increased markedly after cold induction. Some of these polypeptides could be related to oleate desatnrase activity or its regulation by temperature.