Purification and characterization of a novel glycoprotein from Streptomyces sp ZX01
Purification and characterization of a novel glycoprotein from Streptomyces sp ZX01
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DOI：
10.1016/j.ijbiomac.2015.04.012
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发表时间：
2015-07-01
影响因子：
8.2
通讯作者：
Feng, Juntao
中科院分区：
文献类型：
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作者：
Zhang, Guoqiang;Han, Lirong;Feng, Juntao
从放线菌Streptomyces sp.ZX01发酵液中分离得到一种新的抗植物病毒糖蛋白GP-1。MALDI-TOF-MS证实GP-1的分子量约为8.5kDa。GP-1是一种热敏糖蛋白，在80 ℃ ~ 100 ℃处理30 min后，抗病毒活性下降。GP-1含有40.23%的N-和O-糖链。FT-IR和NMR谱证明GP-1含有蛋白质和碳水化合物部分，并含有α-D-（1，6）-葡萄糖残基。圆二色谱分析表明GP-1是一种无序含量较大的糖蛋白。并采用MALDI-TOF-MS和Mascot搜索法对蛋白质序列进行了预测。这些结果表明，糖蛋白GP-1可作为一种新型的天然抗病毒剂应用于农业生产。(C)2015 Elsevier B. V.版权所有。
A novel glycoprotein GP-1 with antiviral activity against plant virus was isolated from the fermentation broth of the actinomycete Streptomyces sp. ZX01. MALDI-TOF-MS proved that molecular weight of GP-1 approximately was 8.5 kDa. GP-1 was a heat-sensitive glycoprotein with decreasing antiviral activity after treated from 80 degrees C to 100 degrees C for 30 min. GP-1 contained 40.23% carbohydrate with N-linked and O-linked glycan. FT-IR and NMR spectra proved that GP-1 contained protein and carbohydrate portions with alpha-D-(1,6)-glucose residues. Circular dichroism revealed that GP-1 was a glycoprotein with a large unordered content. Moreover, protein sequencing was predicted by using MALDI-TOF-MS and Mascot search. These results suggested that glycoprotein GP-1 could be used as a novel natural antiviral agent in agricultural industry. (C) 2015 Elsevier B.V. All rights reserved.