It has a bright band about 50 ku by SDS - PAGE analysis.
通过SDS -PAGE 分析,在50ku处有一目的分子大小的亮带.
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SDS - PAGE analyzed the purity of protein through the purification of Ni - NTA resin.
将包涵体抽提后通过蛋白复性技术使之复性,用Ni -NTA 树脂纯化出目标蛋白,SDS-PAGE电泳分析其纯度达到90%以上.
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The molecular weight of the determinant was 17500 Dalton by SDS - PAGE analysis.
经过SDS -PAGE 电泳分析,这个含有抗原决定簇的蛋白质片段分子量为17500道尔顿,斑点免疫试验证实该片段具有生物学活性.
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SDS - PAGE revealed that the exacted collagen was of high purity.
SDS -PAGE 电泳分析结果显示,所提取的胶原蛋白纯度较高.
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Objective To establish a quick and easy method for SDS - PAGE protein staining.
目的建立一种快速,简易的SDS-PAGE染色方法.
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Figure 2 : SDS - PAGE analysis of purified glucose oxidase.
图 2: 利用SDS -PAGE 分析纯化后的葡萄糖氧化酵素.
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SDS - PAGE showed that the fused protein of interest has been specifically expressed as 61 kD.
所得菌体总蛋白经SDS -PAGE 分析,结果表明,在预期的61kD处 得到一条特异带,为AK( 1-3)cDNA与 载体固有基因DHFR-6хHis的重组蛋白表达产物.
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Colt JM 109 was about 31 . 7 % of the total bacterial products detected by 12 % SDS - PAGE.
用12%SDS - PAGE检测 在 30kD 左右有新生蛋白条带出现,表达量约占菌体总蛋白的31.7%.
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The polymerization of whey protein isolate ( WPI ) at different conditi ons by microbial transglutaminase ( MTGase ) was studied using SDS - PAGE .
采用SDS -PAGE 分析,研究了不同条件下微生物转谷氨酰胺酶 ( MTGase ) 催化乳清蛋白 ( WPI ) 聚合.
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Its molecular weight was 12,600 Dalton by SDS - PAGE and its isoelectric point was 9.8 by IEF.
经SDS -PAGE 测得该抗菌蛋白的分子量为12,600道尔顿,IEF测得其等电点为9.8.
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The supersonic lycate which are assayed on SDS - PAGE geL include the recombined fusion ODF protein.
超声裂解细菌,SDS -PAGE 鉴定裂解物中是否含有重组融合ODF蛋白.
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BL 21 and an expected 14×103 fusion protein was isolated by SDS - PAGE.
重组原核表达质粒 pET28a -COP转化大肠杆菌BL21后,经IPTG诱导表达,获得一条约14×103的融合蛋白.
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After induction, a 52 kDa new protein band appeared in SDS | PAGE.
SDS?PA GE显示一52kDa的诱导产物.
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Its molecular weight was determined to be 45 000 ±2 000 dalton by SDS - PAGE.
经SDS - 凝胶电泳测得分子量为45000±2000.
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The purity of SED using this procedure was 98 %.
毒素纯度为98%,回收率89%,p17.6,MW28500,SDS-PAGE上1条带.
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