Da. Gray et Rgo. Kekwick, OLEATE DESATURASE ACTIVITY IN SUNFLOWER (HELIANTHUS-ANNUUS) SEEDS ANDITS RELATION TO ASSOCIATED CONSTITUENTS DURING SEED DEVELOPMENT, PLANT SCI, 115(1), 1996, pp. 39-47
The locus and specific activity of oleate desaturase (ODS) activity of
developing sunflower seeds has been studied using differential centri
fugation. The ratio of activity recovered in the crude pellet, oil bod
y and microsomal fractions was consistently about 3:1:2 throughout see
d development. Microsomes always contained the highest specific activi
ty of the enzyme, reaching a maximum at 20-25 days after flowering and
declining rapidly thereafter. The change in desaturase specific activ
ity (in vitro) with seed development slightly preceded linoleate accum
ulation (in vivo) but was synchronous with the changing levels of cyto
chrome b. Although the associated metabolic enzymes CDP-choline:1,2-di
acylglycerol cholinephosphotransferase (CPT) and acyl-CoA:lysophosphat
idylcholine acyltransferase (LPCAT) reached maximum activities at the
same time as the desaturase enzyme, these activities decreased less ma
rkedly during subsequent seed maturation. An unrelated microsomal enzy
me, NADPH-cytochrome c-reductase (NCR), did not reach maximal activiti
es until 40 days after flowering.