Partial purification and N-terminal amino acid sequencing of a β-1,3-glucanase from sorghum leaves

R. Velazhahan*, J. Jayaraj, G. H. Liang, S. Muthukrishnan

*المؤلف المقابل لهذا العمل

نتاج البحث: المساهمة في مجلةمراجعة النظراء

8 اقتباسات (Scopus)

ملخص

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.

اللغة الأصليةEnglish
الصفحات (من إلى)29-33
عدد الصفحات5
دوريةBiologia Plantarum
مستوى الصوت46
رقم الإصدار1
المعرِّفات الرقمية للأشياء
حالة النشرPublished - 2003
منشور خارجيًانعم

ASJC Scopus subject areas

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