A subtilisin-like protease was identified in the low-density microsomal fra
ction of developing tung seeds. The abundance of the protease changed signi
ficantly throughout seed development and showed a direct temporal correlati
on with accumulation of storage oil. Once storage oil synthesis was complet
e, the abundance of the protease decreased dramatically. Determination of t
he N-terminal amino, acid sequence revealed that the protease sequence bega
n just after a conserved pro-domain cleavage site, suggesting that the prot
ease was fully active in developing tissue. Extraction of microsomal membra
nes with high salt or pH demonstrated that the protease was not a membrane-
anchored protein.