Journal of Plant Research

, Volume 108, Issue 4, pp 463–468

Purification of cationic peroxidases bound ionically to the cell walls from the roots ofZinnia elegans

  • Yasushi Sato
  • Munetaka Sugiyama
  • Takashi Takagi
  • Hiroo Fukuda
Original Articles

DOI: 10.1007/BF02344235

Cite this article as:
Sato, Y., Sugiyama, M., Takagi, T. et al. J. Plant Res. (1995) 108: 463. doi:10.1007/BF02344235

Abstract

Cell wall-bound and tracheary element-specific peroxidase isoenzymes, designated P5A and P5B, were shown previously to be associated with lignification during the differentiation into tracheary elements of single cells isolated from the mesophyll ofZinnia elegans (Satoet al. Planta 189: 584–589, 1993; Planta 196: 141–147, 1995). Isoenzymes corresponding to P5 (RP5A and RP5B) were present at a relatively high level in the roots ofZinnia elegans. These isoenzymes were purified from theZinnia roots by several column-chromatographic steps. Both RP5A and RP5B had molecular masses of 35 kDa. Purified RP5A and RP5B were cleaved by CNBr and the partial amino acid sequences of these isoenzymes were determined.

Key words

Amino acid sequenceLignificationPeroxidase isoenzymesTracheary element differentiationZinnia elegans

Abbreviations

CAPS

3-cyclohexylaminopropanesulfonic acid

CBB

Coomassie Brilliant Blue R-250

DAB

diaminobenzidine

kDa

kilodalton

PAGE

polyacrylamide gel electrophoresis

PVDF

polyvinylidene difluoride

SDS

sodium dodecyl sulfate

TE

tracheary element

Copyright information

© The Botanical Society of Japan 1995

Authors and Affiliations

  • Yasushi Sato
    • 1
  • Munetaka Sugiyama
    • 1
  • Takashi Takagi
    • 1
  • Hiroo Fukuda
    • 1
  1. 1.Biological Institute, Faculty of ScienceTohoku UniversitySendaiJapan
  2. 2.Department of Biology, Faculty of ScienceEhime UniversityMatsuyamaJapan