Biologia Plantarum

, Volume 46, Issue 1, pp 29–33

Partial Purification and N-Terminal Amino Acid Sequencing of a β-1,3-Glucanase from Sorghum Leaves

Authors

  • R. Velazhahan
    • Department of Plant PathologyTamil Nadu Agricultural University
  • J. Jayaraj
    • Department of BiochemistryKansas State University
  • G.H. Liang
    • Department of AgronomyKansas State University
  • S. Muthukrishnan
    • Department of BiochemistryKansas State University
Article

DOI: 10.1023/A:1022345713761

Cite this article as:
Velazhahan, R., Jayaraj, J., Liang, G. et al. Biologia Plantarum (2003) 46: 29. doi:10.1023/A:1022345713761

Abstract

A protein with an apparent molecular mass of 30 kDa that cross-reacts with barley glucanase antiserum was detected in healthy leaves of sorghum (Sorghum bicolor (L.) Moench). When sorghum leaves were infected with Exserohilum turcicum, the causal agent of leaf blight, the 30-kDa glucanase was substantially induced. The 30-kDa glucanase was partially purified from sorghum leaves using ammonium sulfate fractionation and anion exchange chromatography on DEAE-sephacel. The N-terminal amino acid sequence of the 30-kDa glucanase shows homology to glucanases of maize, barley, bean, soybean, tobacco and pea. The purified 30-kDa glucanase showed antifungal activity against Trichoderma viride.

pathogenesis-related protein Sorghum bicolor Trichoderma viride

Copyright information

© Kluwer Academic Publishers 2003