柱電泳 的英文怎麼說
中文拼音 [zhùdiànyǒng]
柱電泳
英文
column electrophoresis-
6 - phosphogluconate dehydrogenase ( 6 - pgadase, ec 1. 1. 1. 44 ) was isolated by homogenate, ammunium sulfate fractionation, deae - sepharose chromatography, blue - sepharose affinity chromatography and gel filtration with sephadex g - 200 from bacillus subtilis, and some properties of the enzyme had been studied. a 113. 8 - fold purification was obtained with a 8. 2 % yield. the purified enzyme moved as a single electrophoretic band in page
將枯草芽孢桿菌超聲波破壁后的粗提取物進行分段鹽析、 deae - sepharose陰離子交換柱層析, blue - sepharosecl - 6b特異結合柱層析和sephadexg - 200凝膠過濾等純化步驟,得到聚丙烯酰胺凝膠電泳為單一蛋白區帶,比活為1 . 46u mg的酶制劑。Two - dimensionalelectrophoresis of self - and cross - pollinated stylar proteins of shatinyu
異交花柱蛋白質的雙向電泳Medium experiments were arranged under uniform design, and then an optimum medium was got accordingly. the culture liquid was centrifugalized at 3, 500r / min for 30min, then ammonium sulfate was added into the supernatant to a final concentration of 30 % to precipitate the others
通過硫酸銨分級沉澱、 deaesephadexa - 50陰離子交換凝膠層析和sephadexg - 75凝膠柱層析對發酵液進行分離和純化,並得到電泳純的酶。Get the inclusion bodies 2 ) western blot analysis of fusion protein expression ( 1 ) electrophoresis ( 2 ) transfer proteins from gel to membrane ( 3 ) blocking ( 4 ) incubation with primary antibody ( 5 ) enzyme conjugate incubation ( 6 ) substrate incubation. 3 ) gst detection module with cdnb enzymatic assay 3 purification of gst fusion proteins 1 the denaturalization of inclusion bodies. 2 purification using glutathione sepharose 4b column wash matrix with 1 pbs, prepare a 50 % slurry for batch purification method, pack column with matrix slurry
三、 gst一hbrp重組蛋白的純化1 .超聲破碎細胞,離心,上清和沉澱進行sds一page電泳分析2 .樣品處理提取包涵體,變性后,加人用pbs平衡過的以utal腸onesepb抓脫4b ,室溫下孵育3 .以utadtionesepharose4b柱純化以utad雲onesepharose4b柱的準備根據毛山lel ,決定純化所需的gll衛ta1如oneseph娜se4b的柱床體積,用預冷的1xpbs清洗cldtathionese戶, se4b ,得到50 %的基質- acetolactate decarboxylase are widely found among bacterial strains but not in other groups of organisms. the enzyme has been demonstrated to be effective for removal of acetolactate and widely used in beer product. in this paper, - acetolactate decarboxylase from bacillus subtilis was purifed to homogeneity from cell extract by ammonium sulfate - fractionation, heat treatment, deae - sepharose fast flow column chromatography
本文對來源於枯草芽孢桿菌( bacillussubtilis ) 3226 - 5的-乙酰乳酸脫羧酶經硫酸銨分級沉澱、熱處理、 deae - sepharosefastflow離子交換柱層析等分離純化步驟,得到sds - paeg電泳純,通過n末端氨基酸序列分析驗證酶蛋白的純度。The isolation and purification of dnaase in the earthworm the earthworm dnaase was purified from the tissue extract of earthworm by denaturing the protein with low ph buffer, high temperature, ammonium sulfate precipitation, deae - cellulose ( de52 ) chromatography and ultra - filter membrane
雙胸蚓組織中dna酶的分離純化雙胸蚓組織粗提取液經過選擇性酸變性、選擇性熱變性、硫酸按分段鹽析、 deae一纖維素( de52 )柱層析、超濾膜分級分離后得到一個電泳純的dna酶。An antifungal protein, named as b16, was purified from the supernatant of the fermentation broth of strain 041381 by 80 % saturation ammonium sulfate, desalt and gel filtration on sephadex g - 75, which with molecular weight at about 30 - 40 kd on the basis of sds - page
菌株041381發酵上清液經70飽和度硫酸銨沉澱,透析脫鹽, sephadexg - 75凝膠過濾層柱,得到活性物質b16 。以sds - page膠為基礎進行電泳分析, b16的分子量為30 - 40kd 。Proteome indicates the proteins expressed by a genome or tissue. the technology of proteomics requires the seperation, indentification of large number of proteins
用於蛋白質分離的雙向凝膠電泳技術是蛋白質組研究的核心,而鑒定技術則是蛋白質組技術的支柱。The brine shrimp he was prepared and purified by 67 % ammonium sulfate precipitation, deae - sepharose fast flow ion - exchange chromatography, and sephacryl column gel - filtration, and its biochemical and enzymological properties were identified in this study. it was found that the deduced molecular weight of he in sds - page is about 98. 5 kda, and its proteolytic activity was optimized at ph of 7. 5 - 8. 5 and at temperature of 40, respectively
我們利用67硫酸銨沉澱、 deae - sepharosefastflow陰離子交換柱層析和sephacryl凝膠過濾柱層析,並以酪蛋白為其蛋白酶水解活性的檢測底物、以卵膜為其卵殼裂解活性的特異性底物,從鹵蟲胚胎孵化液中分離純化出了鹵蟲的孵化酶分子,其在sds - page電泳中的分子量約為98 . 5kda 。The crude cellulases from liquid fermentation of b - 6 and ass. 3711 were isolated and purified by ( nh4 ) so4 precipitation, sephadex g - 100 and deae - sepharose cl 6b column chromatography. the cmcase components were purified and some of their physical and chemical properties were studied
本文將液體發酵的酶液經硫酸銨分級沉澱、柱層析后得電泳純cmcase組分,並對as3 . 3711和b - 6來源的cmcase酶解動力學和理化性質作了比較研究。By gel filtration on sepharose cl - 6b and cellulose acetate pellicle electrophoresis test, hpa and hpb were respectively a single strait symmetry apex and the result of electrophoresis assume a single spectrum strip
經sepharosecl - 6b柱層析和醋酸纖維素薄膜電泳檢驗, hpa和hpb均為單一狹窄對稱峰且電泳呈單一譜帶。The molecule weight of the 6 - pgadase is 110000da, which is measured by akta fplc and the molecule weight of subunit is 51000da, which is measured by sds - page. therefore one 6 - pgadase has two same subunits
用sephacryls - 300柱( aktafplc系統)測得全酶相對分子質量為110000da ,用sds -聚丙烯酰胺凝膠測得電泳亞基相對分子質量為51000da 。分享友人