详细记录  
题名:Isolation and characterization of a novel thermostable non-specific lipid transfer protein-like antimicrobial protein from motherwort (Leonurus japonicus Houtt) seeds
作者:Xingyong Yang, Jun Li, Xianbi Li, Rong She and Yan Pei
来源:Peptides, Volume 27, Issue 12, December 2006, Pages 3122-3128
URL :http://dx.doi.org/10.1016/j.peptides.2006.07.019
日期:061130
摘要:Xingyong Yang, a, , Jun Li1, a, Xianbi Lia, Rong Shea and Yan Pei, a,

aKey Laboratory of Biotechnology and Crop Quality Improvement, Ministry of Agriculture of China and Biotechnology Research Center, Southwest University, Chongqing 400716, PR China


Abstract

In screening for potent antimicrobial proteins from plant seeds, a novel heat-stable antimicrobial protein, designated LJAMP2, was purified from seeds of the motherwort (Leonurus japonicus Houtt), a medicine herb, with a procedure involving cation exchange chromatography on a CM FF column, and reverse phase HPLCs on C8 column and C18 column. LJAMP2 exhibited a molecular mass of 6.2 kDa determined. Automated Edman degradation determined the partial N-terminal sequence of LJAMP2 to be NH2-AIGCNTVASKMAPCLPYVTGKGPLGGCCGGVKGLIDAARTTPDRQAVCNCLKTLAKSYSG, which displays homology with plant non-specific lipid transfer proteins (nsLTPs). In vitro bioassays showed that LJAMP2 inhibits the growth of a variety of microbes, including filamentous fungi, bacteria and yeast. The growth of three phytopathogenic fungi, Alternaria brassicae, Botrytis maydis, and Rhizoctonia cerealis, are inhibited at 7.5 μM of LJAMP2, whereas Bacillus subtilis is about 15 μM. The IC50 of LJAMP2 for Aspergillus niger, B. maydis, Fusarium oxysporum, Penicillium digitatum and Saccharomyces cerevisiae are 5.5, 6.1, 9.3, 40.0, and 76.0 μM, respectively.

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