Purification of the autotransporter protein Hbp of Escherichia coli.

Purification of the autotransporter protein Hbp of Escherichia coli.
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大肠杆菌自转运蛋白Hbp的纯化。

DOI:
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发表时间:
2001
影响因子:
2.1
通讯作者:
B. Otto
B. Otto
中科院分区:
生物学4区
文献类型:
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作者:
S. J. V. van Dooren;J. Tame;J. Luirink;B. Oudega;B. Otto

文献摘要

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致病性大肠杆菌菌株 EB1 的 Hbp(血红蛋白蛋白酶)已通过凝胶过滤色谱法纯化至均质。纯化的蛋白质能够结合血红素并显示出血红蛋白蛋白酶活性。我们的纯化方法不仅适用于 Hbp,也适用于其他自转运蛋白,并将有助于更好地理解该蛋白家族的功能结构关系。
The enzyme Hbp (hemoglobin protease) of the pathogenic Escherichia coli strain EB1 has been purified to homogeneity by gel filtration chromatography. The purified protein is capable of binding heme and shows hemoglobin protease activity. Our method of purification is applicable not only to Hbp but also to other autotransporter proteins and will contribute to a better understanding of the function-structure relationship of this family of proteins.