Biologia Plantarum

, Volume 46, Issue 1, pp 29-33

First online:

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

  • R. VelazhahanAffiliated withDepartment of Plant Pathology, Tamil Nadu Agricultural University
  • , J. JayarajAffiliated withDepartment of Biochemistry, Kansas State University
  • , G.H. LiangAffiliated withDepartment of Agronomy, Kansas State University
  • , S. MuthukrishnanAffiliated withDepartment of Biochemistry, Kansas State University

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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