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carrier protein molecule
相关语句
  承载蛋白
     the second method: the rare codons in the rLL-37 gene sequence were substituted by the preferred codons of procaryotic cell, and a fragment of carrier protein molecule (CPM) was added to the N termination of the objective sequence to construct expression plasmid pET-30a(+)-CPM-rLL-37, then the rLL-37 was expressed in E. coli. BL21 Star(DE3) and purified by chromatography.
     ②将编码rLL-37基因序列中的部分原核细菌稀有密码子替换为原核细菌偏爱密码子,并在其N端加入一段编码带负电荷的承载蛋白(carrierproteinmolecule,CPM)基因序列,构建表达质粒pET-30a(+)-CPM-rLL-37,并于工程菌BL21Star(DE3)中融合表达、纯化。
短句来源
     Objective To design a carrier protein molecule which can express peptide antibiotics hPAB β at high level.
     目的 通过设计一个承载蛋白分子高效表达肽抗生素hPAB β ,为大量制备hPAB β奠定基础。
短句来源
  承载蛋白分子
     Objective To design a carrier protein molecule which can express peptide antibiotics hPAB β at high level.
     目的 通过设计一个承载蛋白分子高效表达肽抗生素hPAB β ,为大量制备hPAB β奠定基础。
短句来源
  相似匹配句对
     protein.
     protein。
短句来源
     The Carrier
     浅谈催化反应中活性组分的载体
短句来源
     Correlation of bone morphogenetic protein and carrier
     骨形态发生蛋白与载体材料的相关性研究
短句来源
     Identification of clenbuterol-carrier protein conjugate
     克仑特罗偶联物的鉴定
短句来源
     The structure of protein molecule has its own characteristics.
     蛋白质分子有着自身所特有的化学、物理结构;
短句来源
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Objective To design a carrier protein molecule which can express peptide antibiotics hPAB β at high level. Methods According to the properties of peptide antibiotics, a 489 bp DNA sequence coding for the carrier protein was designed under the help of DNAStar software. An expression plasmid pQE CH was constructed by inserting the fusion gene of designed DNA and peptide antibiotics hPAB β into pQE 32 plasmid. After the plasmid was transformed into E. coli JM109, 4 positive recombinants...

Objective To design a carrier protein molecule which can express peptide antibiotics hPAB β at high level. Methods According to the properties of peptide antibiotics, a 489 bp DNA sequence coding for the carrier protein was designed under the help of DNAStar software. An expression plasmid pQE CH was constructed by inserting the fusion gene of designed DNA and peptide antibiotics hPAB β into pQE 32 plasmid. After the plasmid was transformed into E. coli JM109, 4 positive recombinants were selected and used to express the fusion proteins. Results All 4 selected recombinants containing the fusion gene of the designed carrier protein sequence and peptide antibiotics hPAB β expressed the fusion protein at high level about 40% to 45% of total cell proteins. Conclusion Expression plasmid pQE CH constructed from the designed carrier molecule and hPAB β expresses peptide antibiotics hPAB β at high level.

目的 通过设计一个承载蛋白分子高效表达肽抗生素hPAB β ,为大量制备hPAB β奠定基础。 方法 根据肽抗生素的特性 ,确立 4条设计原则 ,并据此设计一 489bp的承载蛋白编码序列 ,用化学合成法获得该序列并将之克隆到pQE 3 2中构建成表达载体 ,进一步将肽抗生素hPAB β基因插入上述表达载体 ,肽抗生素基因位于承载蛋白编码序列 3’ 端 ,两者构成融合基因。将含融合基因的表达载体转化大肠杆菌JM10 9,筛选阳性重组子 ,并用阳性重组子表达融合蛋白。结果 设计的承载蛋白为 163个氨基酸 ,分子量 17668.80 ,等电点 5 .62 1。用承载分子与肽抗生素hPAB β构建的融合蛋白表达载体转化细菌后 ,筛选到 4个阳性重组子 ,均能高效表达肽抗生素融合蛋白 ,融合蛋白的产量占细菌总蛋白的 40 %~ 45 %。结论 设计的承载蛋白分子能够实现肽抗生素的高效表达。

Objective To employ 2 approaches to construct and express reconstructed LL-37 (rLL-37) in procaryotic system, and to explore a better preparation method. Methods The first method: the rLL-37 was inserted into vector pET-28a (+), then was induced to express in E.coli. BL21 (DE3) and purified by chromatography; the second method: the rare codons in the rLL-37 gene sequence were substituted by the preferred codons of procaryotic cell, and a fragment of carrier protein molecule (CPM) was added to the N termination...

Objective To employ 2 approaches to construct and express reconstructed LL-37 (rLL-37) in procaryotic system, and to explore a better preparation method. Methods The first method: the rLL-37 was inserted into vector pET-28a (+), then was induced to express in E.coli. BL21 (DE3) and purified by chromatography; the second method: the rare codons in the rLL-37 gene sequence were substituted by the preferred codons of procaryotic cell, and a fragment of carrier protein molecule (CPM) was added to the N termination of the objective sequence to construct expression plasmid pET-30a(+)-CPM-rLL-37, then the rLL-37 was expressed in E.coli. BL21 Star(DE3) and purified by chromatography. The productive rates of the 2 methods were compared and the antimicrobial effects of obtained rLL-37 was studied. Results The first method: the DNA sequence of rLL-37 was obtained successively by Touch-Down PCR. The expression plasmid pET-30a(+)-CPM-rLL-37 was expressed with fusion protein in E.coli BL21 (DE3). The expression rate accounted for 20% of total bacterio-protein, then the expressed product was purified by using high positive ion exchange column Macro-Prep High S; The second method: a fragment of carrier protein molecule was designed that contained 28 amino-acid residue and its pHi was 2.7, net charge was-6.0 at pH 7.4. After the expression plasmid pET-30a(+)-CPM-rLL-37 was constructed successively, it was expressed in E.coli BL21 Star (DE3). The expressed fusion protein accounted for 35% of total bacterio-protein, then the expressed product was purified by using affinity binding chromatography with TALON resins successfully. The obtained 2 kinds of rLL-37 were able to kill both Gram-negative and-positive bacteria by the means of inhibitory zone. Conclusion It’s feasible to prepare efficiently rLL-37 in procaryotic system, which founds the basis for the further research on bactericidal activity of rLL-37.

目的将改良人源杀菌肽LL-37(rLL-37)用两种方法构建,并分别在原核细胞中融合表达,以寻找较好的制备方法。方法①将编码rLL-37基因序列放入载体pET-28a(+),构建表达质粒pET-28a(+)-rLL-37,并于工程菌BL21(DE3)中融合表达、纯化;②将编码rLL-37基因序列中的部分原核细菌稀有密码子替换为原核细菌偏爱密码子,并在其N端加入一段编码带负电荷的承载蛋白(carrierproteinmolecule,CPM)基因序列,构建表达质粒pET-30a(+)-CPM-rLL-37,并于工程菌BL21Star(DE3)中融合表达、纯化。对比上述2种方法rLL-37的制备率,并初步研究其抗菌性。结果通过Touch-DownPCR法成功获得rLL-37多肽的DNA序列,质粒pET-28a(+)-rLL-37于杆菌BL21(DE3)中表达,融合蛋白约占全菌蛋白的20%,并成功由强阳离子交换柱芯Macro-PrepHighS纯化;设计了一段含28个氨基酸残基的CPM(pHi2.7、pH7.4时电荷为-6.0),成功构建表达质粒pET-30a(+)-CPM-rLL-37,并于杆菌BL21star(...

目的将改良人源杀菌肽LL-37(rLL-37)用两种方法构建,并分别在原核细胞中融合表达,以寻找较好的制备方法。方法①将编码rLL-37基因序列放入载体pET-28a(+),构建表达质粒pET-28a(+)-rLL-37,并于工程菌BL21(DE3)中融合表达、纯化;②将编码rLL-37基因序列中的部分原核细菌稀有密码子替换为原核细菌偏爱密码子,并在其N端加入一段编码带负电荷的承载蛋白(carrierproteinmolecule,CPM)基因序列,构建表达质粒pET-30a(+)-CPM-rLL-37,并于工程菌BL21Star(DE3)中融合表达、纯化。对比上述2种方法rLL-37的制备率,并初步研究其抗菌性。结果通过Touch-DownPCR法成功获得rLL-37多肽的DNA序列,质粒pET-28a(+)-rLL-37于杆菌BL21(DE3)中表达,融合蛋白约占全菌蛋白的20%,并成功由强阳离子交换柱芯Macro-PrepHighS纯化;设计了一段含28个氨基酸残基的CPM(pHi2.7、pH7.4时电荷为-6.0),成功构建表达质粒pET-30a(+)-CPM-rLL-37,并于杆菌BL21star(DE3)中表达,融合蛋白约占全菌蛋白的35%,并被TALON亲和柱芯有效纯化。经抑菌圈实验证明两种方法所获得的rLL-37多肽对G+、G-菌都具有较好的杀菌力。结论rLL-37在原核细胞中的高效表达,为深入研究rLL-37的杀菌活性奠定了基础。

 
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