Molecular Characterization and Expression Analysis of Ascorbate Peroxidase in Codonopsis lanceolata (S. et Z.) Trautv

  • In Jun-Gyo (Biopia Co., Ltd.) ;
  • Lee Eun-Kyung (Biopia Co., Ltd.) ;
  • Kim Ha-Na (Dept. of Oriental Medicine Material and Processing, Kyung Hee University) ;
  • Yoon Jae-Ho (College of Agriculture and Life Sciences, Sunchun National University) ;
  • Lee Mee-Sook (College of Food and Nutrition, Hannam University) ;
  • Yang Deok-Chun (Dept. of Oriental Medicine Material and Processing, Kyung Hee University)
  • Published : 2005.12.01

Abstract

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 ($78{\sim}83%$), 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.

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