抄録
NADP-dependent farnesol dehydrogenase was isolated from black rot fungus-infected sweet potato root tissue and purified almost to homogeneity with several purification steps including Toyopearl HW-60(S) chromatography. The enzymewas estimated to have a molecular weight of 90, 000 and consists of two identical subunits. trans, trans-Famesol was oxdized to trans, transfarnesal at the highest level amongvarious kinds of alcohol in the presence of NADPby the enzyme, but the enzyme showed broad substrate specificity. The SH-group in the enzyme participated in its activity. The enzymewas present in small amounts in fresh tissue, but in response to the infection the activity was increased, accompanied with the accumulation of furanosesquiterpenoids. The activity was increased also in response to cut injury, although in a lesser amount.
