抗体采用蛋白a和肽亲和层析法纯化。
Antibodies are purified by protein a and peptide affinity chromatography.
研究了应用金属螯合亲和层析法纯化重组类人胶原蛋白的条件。
Recombinant human-like collagen with a hexahistidine tail attacked to the carboxyl end could be easily purified by Metal Chelated Affinity Chromatography (MCAC).
本文采用亲和层析法纯化的兔抗64DP抗体,建立了简便灵敏的酶免疫测定法(ELISA)。
We have established a rapid and sensitive method-ELISA for quantitative assay of 64DP. 24 samples were parellelly examined by ELISA and rocket electrophoresis.
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.
结论用尼龙滤膜zbm改进的膜亲和层析法,可用于纯化腹水中的单克隆抗体,且简便、省时、有效。
Conclusion The modified MAC with ZBM is a much easier, time-saving and effective method for affinity purification of antibodies in ascites.
包涵体蛋白经含8m尿素的结合缓冲液溶解后,用金属亲和层析法进行纯化,获得了高纯度的目的蛋白。
After dissolution of inclusion bodies in binding buffer containing 8m Urea, the fusion protein was purified with metal affinity chromatography column, high purity protein was achieved.
利用DEAE离子交换和atp亲和层析法从热休克的大鼠肝脏中分离纯化了热休克蛋白70 (HSP70)。
Heat shock protein 70 (HSP70) was purified from rat liver with DEAE ion exchange chromatography and ATP-affinity chromatography.
结论肺癌相关抗原n 35是一种重要的肿瘤相关抗原,其功能很可能与肿瘤细胞无限制增殖活动有关。麦芽凝集素亲和层析法是纯化肺癌相关蛋白n 35简便有效的途径。
ConclusionThe lung cancer associated antigen N35 might be an important tumor associated antigen and related with the proliferation of cancer cells as a role of tumor cell growth regulator.
用高速离心、分段盐析、亲和层析、超滤和阴离子交换层析法,从牛胎盘中分离纯化出一种肝细胞生长因子。
A kind of hepatocyte growth factor was purified from cow placenta through high speed centrifugation, salting out, affinity chromatography, ultrafiltration and anion exchange chromatography.
表达产物用亲和层析一步法进行纯化,然后用凝胶阻滞试验观察重组蛋白结合质粒的能力。
The expressed protein was purified by one-step affinity chromatography, and its ability of binding plasmid was investigated via gel retardation experiments.
表达产物用亲和层析一步法进行纯化,然后用凝胶阻滞试验观察重组蛋白结合质粒的能力。
The expressed protein was purified by one-step affinity chromatography, and its ability of binding plasmid was investigated via gel retardation experiments.
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