Abstract
The seed storage globulins from sixHelianthus and four hybrids were studied using mono and bidimensional gel SDS electrophoresis (+ 2 mercaptoethanol). The αβ polypeptide composition of each subunit was determined. Different αβ pairs are specifically expressed according to the species studied. Three typical patterns were discriminated. All the studied species exhibit five subunits: two of them are expressed in all the species (α′1β′1 and α′2β′2). The subunit corresponding to the α1β1 pair is present inH. petiolaris and in the three populations ofH. annuus studied. The α2bβ2 pair is common toH. annuus andH. argophyllus. H. petiolaris presents two specific α2aβ2 and α4β′4 pairs andH. annuus a specific α3β′3 pair. InH. argophyllus α1β1 α3β′3 or α4β′4 are never observed but are replaced by α1β′3 and α3β1 pairs. Some globulins, poorly represented, are of αβ′ forms but present α chains of higher molecular weights (in the range 54–56 kDa). Expressing variations in the banding patterns between these species by the use of a similarity index reveals complete identity between the three populations ofH. annuus. Identity between the twoH. petiolaris studied is also observed.H. annuus andH. argophyllus appear to be closer to each other thanH. petiolaris concerning the seed storage globulins.
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Raymond, J., Mimouni, B. & Azanza, JL. Variability in the 11S globulin fraction of seed storage proteins ofHelianthus (Asteraceae). Pl Syst Evol 193, 69–79 (1994). https://doi.org/10.1007/BF00983541
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DOI: https://doi.org/10.1007/BF00983541