A laccase-like activity is correlated with lignin biosynthesis in Zinnia elegans
- Univ. of Georgia, Athens (United States)
The authors have previously shown that a laccase (p-diphenol:O[sub 2] oxidoreductase, EC 1.10.3.1) purified from suspension cultures of Acer pseudoplatanus polymerizes monolignols to form water-insoluble, lignin-like polymers (Sterjiades et al. Plant Physiol. 99:1162). Using chromogenic substrates suitable for staining Acer laccase, we have followed the development of a laccase-like activity in lignifying tissues of Zinnia elegans. We have also used a variety of compounds to examine these same tissues for peroxidase activity, as well as hydrogen peroxide generation. Although peroxidase activity was detected throughout Zinnia stem tissues, evidence will be presented to suggest that the laccase-like activity is more specifically correlated with lignification of vascular tissues during normal development than is peroxidase activity. We are working to characterize the enzyme extracted from Zinnia tissues to determine whether it is indeed a true laccase or some other phenoloxidase. In addition, we are attempting to examine the developmental sequence of Zinnia laccase expression using gene probes and specific antibodies developed against the laccase purified form A. pseudoplatanus.
- DOE Contract Number:
- FG02-92ER20082
- OSTI ID:
- 6247975
- Report Number(s):
- CONF-9307119-; CODEN: PLPHAY
- Journal Information:
- Plant Physiology; (United States), Vol. 102:1; Conference: 1993 joint annual meeting of the American Society of Plant Physiologists (ASPP) and the Canadian Society of Plant Physiologists (CSPP), Minneapolis, MN (United States), 31 Jul - 4 Aug 1993; ISSN 0032-0889
- Country of Publication:
- United States
- Language:
- English
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