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class="vcenter" onerror="javascript:this.src='/static/new_net_01/images/nopic.jpg';"></p></div></div><div id="aipr239" class="smallimg"><div><p class="pic"><img src="http://tyunfile.71360.com/UpLoadFile/szyss/2020/1/637138171486404346/6371381714864043466859489.jpg" class="vcenter" onerror="javascript:this.src='/static/new_net_01/images/nopic.jpg';"></p></div></div></div><div id="m3ovmts" class="content"><p><span>需求數量：</span>0</p><p><span>價格要求：</span>面議</p><p><span>所在地：</span>江蘇省</p><p><span>包裝要求：</span><span style="color: #f30;"></span></p><p><span>產品關鍵詞：</span>北京專業(yè)蛋白純化系統(tǒng)廠家報價,蛋白純化系統(tǒng)</p><p><span>***更新：</span>2020-10-29 23:09:36</p><p><span id="click" >瀏覽次數：0次</span></p><a rel="nofollow" class="button">聯(lián)系我們</a></div></div><div id="b2lxul4" class="rightbox"><h3>公司基本資料信息</h3><p style="border:0;"><a rel="nofollow">蘇州英賽斯智能科技有限公司</a></p><p><span>聯(lián)系人：</span>李大為</p><p><span>郵箱: </span>570745634@qq.com</p><p><span>電話: </span>18606243033</p><p><span>傳真: </span>0512_63937379</p><p><span>網址: </span>http://www.inscinstech.com.cn</p><p><span>手機: </span>0512-63937378</p><p><span>地址: </span>吳江經濟技術開發(fā)區(qū)聯(lián)楊路南側、龍橋路西側</p><p>[當前離線] <a rel="nofollow"> [加為商友] </a><a rel="nofollow"> [發(fā)送信件] </a></p></div></div><div id="v7ne8zg" class="page-proshow02"><p class="title">詳細說明</p><div id="th8subf" class="box"><p><p> 蛋白質純化方法-親和層析親和層析法包括特異性配體親和層析法以及通用性配體親和層析法。比較這兩種親和層析法。特異性配體親和層析法通常將復雜的生命大分子物質作為配體，它的結合力比較大河吸附選擇性比較強。而通用性配體親和層析法通常將簡單的小分子物質作為配體，因此，它具有低廉的成本，吸附容量比較高，通過對吸附和脫附條件的改善能夠使得層析的分辨率提高。原理親和層析的原理類似于酶-底物，***-受體與抗原-抗體等特異性反應的機理。有一定的親和力在每對反應物之間。與在酶與底物的反應中，只有特異的底物才可以結合一定的酶，使復合物產生相同。在親和層析中，只有特異的配體才可以和一定的生命大分子有親和力，北京專業(yè)蛋白純化系統(tǒng)廠家報價，并且使復合物產生，北京專業(yè)蛋白純化系統(tǒng)廠家報價。親和層析配體呈固相，而酶與底物的反應底物呈液相是它們的不同點。事實上，親和層析是在含有活化基團的基質M上以共價鍵的方式固化具有識別能力的配體L，將固相載體制作成功而固化后的配體束縛特異物質的能力依然保持。所以當在小層析柱裝入固相載體，使得欲分離的樣品在該柱經過，北京專業(yè)蛋白純化系統(tǒng)廠家報價。此時，樣品中對配體有親和力的物質S就能夠通過結構互補效應、范德瓦爾力與靜電引力等作用在固相載體上吸附著。北京專業(yè)蛋白純化系統(tǒng)廠家報價</p><div style="width:100%;text-align: center;"><img style="max-width: 640px; max-height: 320px;" alt="北京專業(yè)蛋白純化系統(tǒng)廠家報價,蛋白純化系統(tǒng)" src="http://tyunfile.71360.com/UpLoadFile/szyss/2020/1/637138171486404346/6371381714864043466859489.jpg"></div><p style="text-indent:25px">蛋白質分離純化步驟（二）分離純化蛋白質的一般程序 2.1 材料的預處理及細胞破碎分離提純某一種蛋白質時，首先要把蛋白質從組織或細胞中釋放出來并保持原來的天然狀態(tài)，不喪失活性。所以要采用適當的方法將組織和細胞破碎。常用的破碎組織細胞的方法有： 1. 機械破碎法這種方法是利用機械力的剪切作用，使細胞破碎。常用設備有，高速組織搗碎機、勻漿器、研缽等。 2. 滲透破碎法這種方法是在低滲條件使細胞溶脹而破碎。 3. 反復凍融法生物組織經凍結后，細胞內液結冰膨脹而使細胞脹破。這種方法簡單方便，但要注意那些對溫度變化敏感的蛋白質不宜采用此法。 4. 超聲波法使用超聲波震蕩器使細胞膜上所受張力不均而使細胞破碎。 5. 酶法如用溶菌酶破壞微生物細胞等。四川蛋白純化系統(tǒng)制造廠家</p><div style="width:100%;text-align: center;"><img style="max-width: 640px; max-height: 320px;" alt="北京專業(yè)蛋白純化系統(tǒng)廠家報價,蛋白純化系統(tǒng)" src="http://tyunfile.71360.com/UpLoadFile/szyss/2020/1/637138171935864644/6371381719358646441189533.jpg"></div><p style="text-indent:25px">三、蛋白質分子量的測定蛋白質分子量測定的方法很多，目前常用的方法有以下幾種。 3.1 凝膠過濾法凝膠過濾法測定蛋白質分子量的原理如“分離純化方法”中所述。一定型號的凝膠顆粒上具有一定大小的孔隙，只允許較小的分子進入膠粒，而大于孔隙的分子則不能進入膠粒而被排阻在膠粒外面。用洗脫液洗脫時，被排阻的分子量大的蛋白質先被洗脫下來，隨后能夠進入顆粒的蛋白質也按分子量大小而先后被洗脫下來，分子量越小的越后被洗脫下來。由于不同排阻范圍的葡聚糖凝膠有一特定的蛋白質分子量范圍，在此范圍內，分子量的對數和洗脫體積之間成線性關系。因此，用幾種已知分子量的蛋白質為標準進行層析分析，以每種蛋白質的洗脫體積對它們的分子量的對數作圖，繪制出標準洗脫曲線。未知蛋白質在同樣的條件下進行層析分析，根據其所用的洗脫體積，從標準洗脫曲線上可求出此未知蛋白質對應的分子量來。</p><p style="text-indent:25px">三、蛋白質分子量的測定 3.3 沉降法沉降法又稱超速離心法。蛋白質溶液在受到強大的離心力作用時，蛋白質分子趨于下沉，沉降速度與蛋白質分子的大小、密度和分子形狀有關，也與溶劑的密度和粘度有關。蛋白質顆粒在離心場中的沉降速度用每單位時間內顆粒下沉的距離來表示。在離心場中，蛋白質分子所受到的凈離心力（離心力減去浮力）與溶劑的摩擦力平衡時，每單位離心場強度的沉降速度稱為沉降系數（Sedimentation Coefficient）。國際上采用Svedberg單位作為沉降系數的單位，用S表示，以紀念超速離心法的創(chuàng)始人，瑞典***的蛋白質化學家T.Svedberg。一個Svedberg單位（或直接稱一個S）為1×10—13s。蛋白質的沉降系數大約在1×10—13～200×10—13s范圍內，即1S～200S。</p><div style="width:100%;text-align: center;"><img style="max-width: 640px; max-height: 320px;" alt="北京專業(yè)蛋白純化系統(tǒng)廠家報價,蛋白純化系統(tǒng)" src="http://tyunfile.71360.com/UpLoadFile/szyss/2020/1/637138172377738528/6371381723777385289828518.jpg"></div><p style="text-indent:25px">蛋白質分離純化步驟（二） 2.2 蛋白質的抽提通常選擇適當的緩沖液溶劑把蛋白質提取出來。抽提所用緩沖液的pH、離子強度、組成成分等條件的選擇應根據欲制備的蛋白質的性質而定。如膜蛋白的抽提，抽提緩沖液中一般要加入表面活性劑（十二烷基磺酸鈉、tritonX-100等），使膜結構破壞，利于蛋白質與膜分離。在抽提過程中，應注意溫度，避免劇烈攪拌等，以防止蛋白質的變性。 2.3蛋白質粗制品的獲得選用適當的方法將所要的蛋白質與其它雜蛋白分離開來。比較方便的有效方法是根據蛋白質溶解度的差異進行的分離。常用的有下列幾種方法： 1. 等電點沉淀法不同蛋白質的等電點不同，可用等電點沉淀法使它們相互分離。 2. 鹽析法不同蛋白質鹽析所需要的鹽飽和度不同，所以可通過調節(jié)鹽濃度將目的蛋白沉淀析出。被鹽析沉淀下來的蛋白質仍保持其天然性質，并能再度溶解而不變性。 3. 有機溶劑沉淀法中性有機溶劑如乙醇、**，它們的介電常數比水低。能使大多數球狀蛋白質在水溶液中的溶解度降低，進而從溶液中沉淀出來，因此可用來沉淀蛋白質。此外，有機溶劑會破壞蛋白質表面的水化層，促使蛋白質分子變得不穩(wěn)定而析出。由于有機溶劑會使蛋白質變性，使用該法時，要注意在低溫下操作.江蘇樣品前處理蛋白純化系統(tǒng)上門安裝</p><p style="text-indent:25px">北京專業(yè)蛋白純化系統(tǒng)廠家報價</p><p style="text-indent:25px">蛋白質分離純化步驟（二） 2.4 樣品的進一步分離純化用等電點沉淀法、鹽析法所得到的蛋白質一般含有其他蛋白質雜質，須進一步分離提純才能得到有一定純度的樣品。常用的純化方法有：凝膠過濾層析、離子交換纖維素層析、親和層析等等。有時還需要這幾種方法聯(lián)合使用才能得到較高純度的蛋白質樣品。 1. 凝膠過濾層析凝膠過濾層析（gel-filtration chromatography）又稱為分子排阻層析或分子篩層析。它是將葡聚糖凝膠（Sephadex）裝入一個柱子中，制成凝膠柱。這種凝膠顆粒具有網狀結構，不同類型凝膠的網孔大小不同。當把蛋白質混合樣品加到凝膠柱中時，比凝膠網孔小的蛋白質可進入網孔內，而大于網孔的分子則不能進入被排阻在凝膠顆粒之外。當用洗脫液洗脫時，被排阻的分子量大的蛋白質直接通過凝膠之間的縫隙先被洗脫下來，而比網孔小的蛋白質可連續(xù)不斷地進入網孔內。這樣的小分子不但流經的路程長，而且受到來自凝膠內部的阻力也很大，所以蛋白質越小，從柱子上洗脫下來所需時間越長。由于不同蛋白質的分子大小不同，進入網孔的程度不同，因此流出的速度不同，洗脫所用體積及時間不同，從而達到分離的目的。北京專業(yè)蛋白純化系統(tǒng)廠家報價</p><p style="text-indent:25px">蘇州英賽斯智能科技有限公司致力于儀器儀表，是一家生產型公司。公司自成立以來，以質量為發(fā)展，讓匠心彌散在每個細節(jié)，公司旗下蛋白純化色譜系統(tǒng)，凝膠凈化色譜系統(tǒng)，制備液相色譜，柱塞泵深受客戶的喜愛。公司從事儀器儀表多年，有著創(chuàng)新的設計、強大的技術，還有一批**的專業(yè)化的隊伍，確保為客戶提供良好的產品及服務。英賽斯立足于全國市場，依托強大的研發(fā)實力，融合前沿的技術理念，飛快響應客戶的變化需求。</p></p><br /><p>文章來源地址: http://www.cdcfah.com/cp/1762567.html</p></div></div></div></div></div><div id="clxuqhg" class="page-right twoColRt"><div id="7yzlc22" class="box01 margin10 clearfix"><h3><a href="http://www.cdcfah.com/cp/">猜你喜歡</a></h3><div id="3lhh2iu" class="recomPic likePro"><a href="http://www.cdcfah.com/cp/814588.html"><div><img 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