purified protein fraction 中文意思是什麼
purified protein fraction
解釋
純化蛋白組分-
By sds - page and immuno - blotting, the monoclonal antibody of anti - chick brain cytoplasmic dynein intermediate chain could recognize the 67 kda protein in purified golgi apparatus fraction from lily pollen. subsequently by immuno - gold labeling and transmission electron microscopy, we found that the dynein intermediate chain - like protein bound mainly to the membranes of golgi - associated vesicles. statistics analysis of dynein intermediate chain - like protein on golgi - associated vesciles showed the nearly equal chance of distribution on either cis - or trans - golgi - associated vesciles
對分離純化的百合花粉及花粉管中高爾基體組分進行sds -聚丙烯酰胺凝膠電泳和免疫印跡發現，抗雞腦細胞質力蛋白中間鏈單克隆抗體在67kda處有較強的免疫交叉反應；進而通過免疫金標結合電子顯微鏡觀察發現，大多數類細胞質力蛋白中間鏈存在於高爾基體附近的囊泡膜上；統計結果表明，類細胞質力蛋白中間鏈在順面和反面高爾基體附近囊泡膜上的分佈機率大致相等。 -
We have sifted 103 medicinal plants, roughly identified 17 plants might contain antifungal proteins. antifungal protein was purified from cassia sophera linn, by extraction, fraction with ( nh _ ( 4 ) ) _ ( 2 ) so _ ( 4 ), cation - exchange chromatography of cm - sepharose ff xk 26, the first cation - exchange chromatography of mono s and the second one, followed by gel filtration of superose 12hr
對茳芒決明進行了抗菌蛋白的分離純化：經粉碎、磷酸緩沖液浸提、硫酸銨沉澱、 cm - sepharoseffxk26陽離子交換層析、兩次monos陽離子交換層析、 superose12hr分子篩層析可得到具抗真菌活性的蛋白。 -
Major difference of hn proteins lies in no. 18 - no. 75 amino acid residues on n - terminal which includes three active sites of hn protein. the influence on biological action, caused by the difference of hn protein, is needed to study further. hn gene has only four glycosylation sites, which is 1 or 2 less on amount than that of other strains. so, this difference can be take on as a natural mark of ndv b95 strain furthermore, the fragment encoding hn gene was excised from the positive clone pgem - hn with sail and saci enzyme, and purified by agrose gel fraction method. then the fragment was subcloned into the pet - 28c expressing vector digested by sail and saci restriction enzyme
作者將正確的重組克隆質粒pgem - hn用saii 、 saci雙酶切，電泳回收目的片段，將其亞克隆到經saii 、 saci雙酶切處理的pet - 28c中，轉化大腸桿菌tgi感受態細胞，得到的轉化子經pcr鑒定和酶切分析，篩選出符合閱讀框的重組子，構建成重組表達質粒pet - hn ，並在大腸桿菌bl _ （ 21 ） （ de _ 3 ）宿主菌中成功地表達了含目的蛋白的融合蛋白，融合蛋白的分子量約66kd ，加入iptg誘導8h后，蛋白表達幾乎達到最高水平。
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