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The study was aimed to investigate the technological parameters of rhIL-11 preparation from fusion protein by using enterokinase.

本研究探讨利用激酶加工融合蛋白的方法制备重组人白细胞介素11(rhIL-11)的工艺条件与参数。

This investigation would be able to lay a foundation for enterokinase activity research and farther application of expression products on a large scale.

该粗酶经脱盐后在适宜的缓冲体系中21℃温育过夜,显示出较高的自催化切割活性,为进一步进行重组牛激酶活性的研究及应用奠定了基础。

After fermentation and product purification, we got some purified fusion protein SOD-Thyα1. And the Enterokinase digestion of fusion protein was also studied.

经发酵和纯化得到了融合蛋白SOD-Thyα1的纯品,并对融合蛋白的激酶切割特性进行了初步研究。

In conclusion, the preparation method of rhIL-11 from fusion protein by using enterokinase is simple and feasible with good separation, which can meet industrial requirements.

利用激酶加工融合蛋白以制备rhIL-11的方法简单可行,分离纯化效果好,能够满足工业生产的需要。

The recombinant mouse enterokinase light chain could be well expressed in Ecoli, but most of them were inclusion.

利用pET32a/BL21(DE3)表达系统成功地在大杆菌中表达了重组鼠源性激酶轻链,表达量约占大杆菌BL21(DE3)总蛋白的30%,但多以包涵体的形式存在。

The inactive precursor of trypsin, produced by the pancreas and converted to trypsin in the small intestine by enterokinase.

胰蛋白酶原胰朊酶的惰性前体;由胰制造并由激酶在小内转化为胰朊酶

Recombinant hK5 with native N-terminus was generated by enterokinase cleavage and affinity chromatography purification.

激酶切割和纯化,获得了与天然蛋白N-末端相同的hK5重组蛋白。

We also inserted an Enterokinase recognition site between the hSOD gene and the small peptide gene, then we can cleave away the small peptide from fusion protein easily.

在构建时还在小分子多肽与人SOD的连接区插入激酶识别位点,这样可以使小分子多肽能从融合蛋白中切割下来。

Having been renaturalized, the fusing protein product is digested with enterokinase, purified by Ni-sepharose and HPLC.

复性、激酶酶切、Ni-Sepharose和HPLC纯化后,用质谱测定其分子量并进行活性测定。

The resulting was cleavaged with Enterokinase afte lectrelution and dialysis to carries on the inhibiting test and demonstrated activated.

对目的条带电洗脱、透析回收、激酶切割后进行抑菌实验,显示有活性。

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