A cytosolic ascorbate peroxidase, hydrogen peroxide-scavenging enzyme, was characterized from Codonopsis lanceolata. The cytosolic ascorbate peroxidase cDNA (CAPX) was 983 nucleotides long and possess an open reading frame of 753 bp with 251 amino acids (MW 27.9 kDa) with pI 5.61. The deduced amino acid sequence of CAPX shows high homology to other known cytosolic APXs (78~83%), but the CAPX was clustered independently from compared ten plant APXs. The CAPX gene was highly expressed in leaf and stem tissues, but not in root. When Codonopsis leaves cut using scalpel were soaked in 1 mM hydorgen peroxide, the expression of CAPX gene was suppressed.

A cinnamoyl CoA reductase (CCR) cDNA (ClCCR) was isolated from tabroot mRNAs of Codonopsis lanceolata by cDNA library construction, and its expression was investigated in relation to abiotic stresses. The ClCCR is 1008 bp in length with an open reading frame (ORF) of 336 amino acids. The deduced amino acid sequence was showed high similarity with cinnamoyl-CoA reductases of P. tremuloides (AAF43141) 87%, F.×aranassa (AAP46143) 83%, L. album (CAD29427) 80%, E. gunnii (CAA66063) 72%, S. tuberosum (AAN71761) 83%. Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis was revealed that the ClCCR expression was regulated by abiotic stresses.