本文论述了基因重组融合蛋白纯化过程和存在的问题。
The paper describes process of recombinant fusion protein in purification and existing problems.
研究目的：克隆表达人肠激酶轻链编码基因，以期应用于融合蛋白的切割与纯化。
Objective: To clone and express the gene of human enterokinase light chain which would be used in the cleavage and purification of fusion proteins.
用谷胱甘肽琼脂糖凝胶4b亲和介质从菌体裂解液中纯化了GST -MBD4融合蛋白。
The GST-MBD4 fusion protein was purified from cell lysates using glutathione Sepharose 4b affinity chromatography.
人神经肽y；融合蛋白；包涵体；纯化；生物信息学。
Neuropeptide y; Fusion protein; Inclusion body; Purification; Bioinformatics.
目的：表达和纯化半乳糖凝集素- 1融合蛋白。
Objective: To express and purify the fusion protein of galectin-1.
菌体经过超声破碎后反复洗涤包涵体，融合蛋白纯度达到70%，进一步用离子交换层析和凝胶过滤层析纯化使其纯度达95%以上。
The purity of fusion protein was about 70% after ultrasonic decomposition and washing repeatedly, and reached above 95 % after purification by ion exchange and gel-filtration chromatography.
融合蛋白基因在巴斯德毕赤酵母中进行表达后通过阳离子交换层析、反向层析和凝胶过滤对表达产物进行了分离纯化。
HSA-AX15(R13K ) fusion protein was purified to homogeneity by cation exchange chromatography, re verse phase chromatography and gel filtration after expressed in pichia pastor is.
发酵菌株，纯化制备融合蛋白。
建立了TSF蛋白的纯化复性方法，获得了GST - TSF融合蛋白及TSF蛋白。
The purification procedure was established, and the purified TSF and its fused protein GST TSF were obtained.
目的：克隆长双歧杆菌ncc 2705株果糖结合蛋白bl 0033的基因，利用大肠杆菌表达GST -BL 0033融合蛋白并纯化。
Objective: to clone the gene of fructose binding protein BL0033 from Bifidobacterium longum NCC2705, and express and purify fusion protein GST-BL0033 in e.
结论：用硫氧还蛋白融合表达系统在大肠杆菌中表达的小鼠内皮抑素重组融合蛋白易纯化并具有高活性。
CONCLUSION: The mouse endostatin recombinant fusion protein expressed in E. coli by using thioredoxin fusion expression system is easy to be purified and possesses high activity.
结论：成功表达纯化并鉴定构建了ESAT - 6融合蛋白。
Conclusion: The ESAT-6 fusion protein was successfully expressed and purified, identified.
蛋白a纯化获得电泳纯融合蛋白。
结论GST-3C蛋白酶不仅可以应用于融合蛋白的酶切，而且为引入3C蛋白酶识别位点的串联亲和纯化（TAP）系统提供又一种酶切工具。
Conclusion The recombinant GST-3C protease can be not only applied to the cleavage of fusion proteins, but also be used as a tool-enzyme in TAP system containing 3C recognition sequence.
结论：构建了8r - MUC1核心肽融合蛋白原核表达载体并成功表达与纯化出具有生物学活性的融合蛋白。
Conclusion the prokaryotic expression vector of 8r-muc1 core peptide fusion protein has been constructed, and the fusion protein with biological activity has been successfully expressed and purified.
以纯化的融合蛋白为抗原免疫家兔制备出了抗血清。
IPTG诱导表达融合蛋白，包涵体蛋白经复性后亲和层析法纯化，ELISA方法测定蛋白活性。
Fusion protein expression was induced by IPTG. After renaturation, the protein was purified by affinity chromatography and the bioactivity was examined by ELISA.
结果：经表达和纯化获得了纯度达90%以上的融合蛋白；
Results: The recombinant proteins were expressed successfully and the purity was over 90% after purified by affinity chromatography.
多肽融合标签能够赋予目标蛋白新的特性，便于目标蛋白的定位、追踪、纯化以及结构和相互作用研究。
Using gene fusion technology, polypeptide fusion tags can be engineered into target proteins at the genetic level.
将纯化之球蛋白片段免疫 BALB/c小鼠后， 取脾脏细胞与小鼠骨髓瘤细胞株 NS-1进行细胞融合。
The splenocytes of immunized BALB/c strain mice with purified Ig were fused with myeloma cell line, NS-1 . The supernatants of hybridoma were screened by ELISA.
通过SDS - PAGE检测融合蛋白的纯度，采用点杂交和纤维蛋白凝结活性检测分析，显示纯化产物具有较高生物活性。
SDS-PAGE was used to detect the purity of target protein. A higher bioactivity of purified products was shown by the determination of dot-blotting assay and fibrinogen-clotting analysis.
目的：构建融合重组表达载体并对其进行诱导表达和蛋白纯化以获得大量重组融合蛋白。
AIM: to construct the recombinant expression vector and to obtain large amount of mouse Cyclin D1 protein fused to PTD.
结论：成功构建了人ip - 10融合蛋白表达载体，并纯化得到具有活性的IP - 10融合蛋白，为进一步研究IP - 10的功能提供了重要的实验材料。
CONCLUSION: We successfully construct IP-10 fusion protein expressing vector and get the fusion protein with high bioactivity, which provides essential materials for the future studies on IP-10.
通过固定化金属亲和层析、阴离子交换、疏水层析融合蛋白得到了纯化，其纯度可达91%。
By immobilized metal affinity chromatography, ion-exchange chromatography and hydrophobic interaction chromatography, the recombinant Gln49-PLA2 was purified with 91% purity.
通过固定化金属亲和层析、阴离子交换、疏水层析融合蛋白得到了纯化，其纯度可达91%。
By immobilized metal affinity chromatography, ion-exchange chromatography and hydrophobic interaction chromatography, the recombinant Gln49-PLA2 was purified with 91% purity.
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