Abscisic acid (ABA) specific-binding sites localized in the cytosol were id
entified and characterized in the flesh of developing apple (Malus pumila L
. cv. Starkrimon) fruit. ABA binding activity was scarcely detectable in th
e microsomes but high ABA binding activity in the cytosolic fraction was de
tected. The ABA-binding sites possessed a protein nature with both active s
erine residues and thiol-groups of cysteine residues in their functional bi
nding sites. ABA binding was shown to be saturable, reversible and of high
affinity. A Scatchard plot provided evidence for two different ABA binding
proteins, one with higher affinity (K-d=2.3 nM) and the other with lower af
finity (K-d=58.8 nM). Phaseic acid, trans-ABA and (-)-ABA had essentially n
o affinity for the binding proteins, indicating their stereospecificity to
bind physiologically active cis-(+)-ABA. The time-course, pH- and temperatu
re-dependence of the ABA-binding proteins were determined. It is hypothesiz
ed that the detected ABA-binding proteins may be putative ABA-receptors tha
t mediate ABA signals during fruit development.