A new assay for the evaluation of spermidine (Spd) synthase activity w
as developed. It involves a coupled reaction and avoids the use of dec
arboxylated S-adenosylmethionine, which is unstable and not easily ava
ilable. This assay was applied to assess changes in enzyme activity in
oat leaves subjected to osmotic stress in the dark. The results indic
ate that osmotically-induced putrescine (Put) accumulation in cereals
results not only from the activation of the arginine decarboxylase pat
hway, but also from the inhibition of the activity of Spd synthase, th
e enzyme which catalyzes the transformation of Put to Spd. Other possi
bilities which could contribute to the decline of Spd and spermine lev
els under osmotic stress are also discussed.