The cDNA of alcohol dehydrogenase (PgADH) was isolated and characterized from the leaf of Panax ginseng. The cDNA had an open reading frame of 801 bp and a deduced amino acid sequence of 266 residues. The calculated molecular mass of the mature protein is approximately 29 kDa with a predicated isoelectric point of 6.84. Homology analysis revealed that the deduced amino acid of PgADH shares a high degree of homology with the short-chain ADH proteins of other plants. Genomic DNA hybridization analysis indicated that PgADH represents a multi-gene family. The expression of PgADH under various environmental stresses was analyzed at different time points using real-time PCR. ABA, SA and especially JA (80-fold) significantly induced PgADH expression within 24 h of treatment. The positive responses of PgADH to abiotic stimuli suggest that ginseng ADH may protect against hormone-related environmental stresses.
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