Oita S, Ohnishi-Kameyama M, Nagata T
Shikoku National Agricultural Experiment Station, Ministry of Agriculture, Forestry and Fisheries, Zentsuji, Kagawa, Japan.
Biosci Biotechnol Biochem. 2000 May;64(5):958-64. doi: 10.1271/bbb.64.958.
An antimicrobial peptide termed BCP-2 was purified from barley grain by chitin-affinity treatment and HPLC. The results of amino acid analysis and mass spectrometry of BCP-2 indicate that the peptide is very similar to barley alpha-thionin. BCP-2 and wheat alpha1-thionin were also bound to beta-glucan but not to starch. The binding of BCP-2 to laminarin (beta-1,3-1,6-glucan) and laminarioligosaccharides was supported by fluorescence polarization data. This is the first report on the binding of alpha-thionins to polysaccharide containing chitin and beta-1,3-glucan, which construct fungal cell walls.
一种名为BCP-2的抗菌肽通过几丁质亲和处理和高效液相色谱法从大麦籽粒中纯化得到。BCP-2的氨基酸分析和质谱结果表明，该肽与大麦α-硫堇非常相似。BCP-2和小麦α1-硫堇也与β-葡聚糖结合，但不与淀粉结合。荧光偏振数据支持了BCP-2与海带多糖（β-1,3-1,6-葡聚糖）和海带寡糖的结合。这是关于α-硫堇与构成真菌细胞壁的含几丁质和β-1,3-葡聚糖的多糖结合的首次报道。
