Shaikh Faiyaz K, Gadge Prafull P, Padul Manohar V, Kachole Manvendra S
Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, Maharashtra India.
Department of Biotechnology, MGM's Institute of Biosciences and Technology, Aurangabad, Maharashtra 431003 India.
3 Biotech. 2018 Jan;8(1):19. doi: 10.1007/s13205-017-1040-y. Epub 2017 Dec 13.
is an orthodox rival of many crop plants affecting agricultural economy. Plant leaves found to accumulate proteinase inhibitors, although this insect pest chooses leaves for laying eggs. Plant defense response at this juncture is not fully explored. In this context, here we are reporting proteinase inhibitor (LPI-1) having significant homology with the I13 family from leaves of pigeonpea (cv. BSMR 736). The isolation of LPI-1 was carried out from leaves of field-grown pigeonpea under an outbreak of . The acetone precipitated LPI-1 (125 µg) displayed substantial inhibition potential towards bovine trypsin (56.5 ± 1.8%) and HaGPs (52.6 ± 1.7%) on solution assay. These results were corroborated with dot-blot analysis. The molecular form of LPI-1 was characterized by reverse zymography and GXCP. The optimum condition was found to be pH 8 and temperature in the range of 30-40 °C. The protein identification via MASCOT-PMF and NCBI-BLAST search showed substantial homology with an inducible subtilisin inhibitor of Fabaceae comprising (96%), (78%), (76%), (75%), (73%) and (73%) consists of conserved domain of potato inhibitor I family.
是影响农业经济的许多农作物的传统竞争对手。尽管这种害虫选择叶子来产卵,但发现植物叶子会积累蛋白酶抑制剂。此时植物的防御反应尚未得到充分研究。在此背景下,我们在此报告从木豆(品种BSMR 736)叶片中分离出的与I13家族具有显著同源性的蛋白酶抑制剂(LPI-1)。LPI-1的分离是在田间种植的木豆叶片爆发[此处原文缺失相关害虫名称]时进行的。丙酮沉淀的LPI-1(125μg)在溶液分析中对牛胰蛋白酶(56.5±1.8%)和HaGPs(52.6±1.7%)显示出显著的抑制潜力。这些结果通过斑点印迹分析得到了证实。LPI-1的分子形式通过反向酶谱法和GXCP进行了表征。发现最佳条件为pH 8和30 - 40°C的温度。通过MASCOT-PMF和NCBI-BLAST搜索进行的蛋白质鉴定显示,与豆科植物的一种可诱导枯草杆菌蛋白酶抑制剂具有显著同源性,该抑制剂包含[此处原文缺失具体成分信息](96%)、[此处原文缺失具体成分信息](78%)、[此处原文缺失具体成分信息](76%)、[此处原文缺失具体成分信息](75%)、[此处原文缺失具体成分信息](73%)和[此处原文缺失具体成分信息](73%),由马铃薯抑制剂I家族的保守结构域组成。