• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Mycologia >Characterization of a neutral serine protease and its full-length cDNA from the nematode-trapping fungus Arthrobotrys oligospora
【24h】

Characterization of a neutral serine protease and its full-length cDNA from the nematode-trapping fungus Arthrobotrys oligospora

机译：捕获线虫的真菌节肢动物寡孢中性丝氨酸蛋白酶及其全长cDNA的特征

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

A neutral serine protease (designated Aoz1) was purified to homogeneity from a strain of Arthrobotrys oligospora, obtained from soil in Yunnan Province. The purified protein showed a molecular mass of approximately 38 000 Dalton, pI 4.9 and displayed optimal activity at 45 C and pH 6-8. The protein could hydrolyze gelatin, casein and the chromogenic substrate azocoll, and it Could immobilize nematodes in vitro (Panagrellus redivivus L. [Goodey]). The level of activity in culture medium was found to increase with increasing gelatin concentration. Scanning electron micrographs demonstrated dramatic structural changes in nematode cuticle treated with the purified protease. A partial peptide sequence obtained by N-terminal sequence analysis was used to design degenerate primers for the isolation of a cDNA gene encoding the mature protease. Analysis of the cDNA and corresponding genomic sequence revealed 97% identity with PII, a gene previously described from A. oligospora, and we conclude that this gene is likely a PII ortholog.
机译：从云南省土壤中获得的节肢动物寡孢菌株中纯化出一种中性丝氨酸蛋白酶（命名为Aoz1）至同质。纯化的蛋白质的分子量约为38 000道尔顿，pI 4.9，并在45 C和pH 6-8下显示最佳活性。该蛋白可以水解明胶，酪蛋白和生色底物azocoll，并且可以在体外固定线虫（Panagrellus redivivus L. [Goodey]）。发现培养基中的活性水平随着明胶浓度的增加而增加。扫描电子显微镜照片显示，用纯化的蛋白酶处理过的线虫表皮具有显着的结构变化。通过N末端序列分析获得的部分肽序列用于设计简并引物，用于分离编码成熟蛋白酶的cDNA基因。 cDNA和相应的基因组序列的分析表明，它与先前从寡孢曲霉（A. oligospora）描述的基因PII具有97％的同一性，因此我们得出结论，该基因可能与PII直系同源。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号