生物化學翻譯
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To show that HAX-1 degradation is part of the apoptotic process and any involvement Omi may have， we used the ucf-101 inhibitor. ucf-101 is a specific inhibitor of the proteolytic activity of Omi and has been described previously (13). When... To show that HAX-1 degradation is part of the apoptotic process and any involvement Omi may have， we used the ucf-101 inhibitor. ucf-101 is a specific inhibitor of the proteolytic activity of Omi and has been described previously (13). When HK-2 cells were treated with cisplatin in the presence of ucf-101， the percentage of apoptotic cells decreased and the inhibitor significantly blocked HAX-1 degradation. This effect was more pronounced when a higher concentration of the inhibitor was used. To confirm the specificity of the inhibitor in this system and exclude the possibility that another protease rather than Omi is involved in HAX-1 cleavage， we used cell lines derived from mnd2 mice (9). The parent cell line (mnd2-MSCV) derived from mouse embryo fibroblasts has no detectable Omi proteolytic activity (9). The same cell line has been transfected with wild type human Omi cDNA (mnd2-MSCV-Omi) and expresses high levels of active Omi protein (14). We found that in mnd2-MSCV cells， when induced to undergo apoptosis with various stimuli， the number of apoptotic cells was very low. Furthermore， no detectable cleavage of HAX-1 was observed. This is in contrast with the mnd2-MSCV-Omi cells where apoptosis was robust， and HAX-1 levels were inversely proportional to the degree of apoptosis. This experiment clearly shows that Omi is solely responsible for HAX-1 cleavage， which is essential for apoptosis under the conditions used in these experiments. HAX-1 subcellular localization depends on cell type (21， 30) and has been reported to be present in the mitochondria， cytoplasm， or plasma membrane (10， 21， 22， 30). We performed subcellular fractionation to investigate where HAX-1 cleavage by Omi takes place. We found that， in HEK293 cells， HAX-1 was predominantly present in the mitochondria， and this localization did not change in response to apoptotic stimuli. This suggests that Omi can initiate apoptosis in the mitochondria by cleaving HAX-1 protein. This is in accord with a recent study that shows Omi can induce apoptosis in human neutrophils treated with TNF- without being released from the mitochondria (7). Although several studies clearly define HAX-1 as an anti-apoptotic protein， the mechanism of its function is unknown. HAX-1 has sequence similarity to Bcl-2 family of proteins (10， 22). 展開
全部評論(1條)
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- go小飛454 2007-02-04 00:00:00
- 為了表明HAX-1 的降解是凋亡過程的一部分以及OMI可能的參與，我們用ucf-101YZ劑。ucf-101是此前報道過的(13)卵母細胞成熟YZ因子蛋白酶解活性的一種特異性YZ劑。當HK-2 細胞在ucf-101的存在下用順鉑處理時，凋亡細胞百分比下降，而且這種YZ劑明顯阻止了HAX-1的降解。當YZ劑濃度加大時這種效應更加突出。 為了證實這種YZ劑在本系統(tǒng)中的特異性，并排除其他蛋白酶而不是OMI 涉及HAX-1酶切的可能性，我們使用mnd2 小鼠衍生的細胞系(9)。小鼠胚胎成纖母細胞系(mnd2-MSCV)沒有可檢測的OMI 蛋白酶活性(9)。相同的細胞系被轉(zhuǎn)染到野生型人類OMI的cDNA (mnd2-MSCV-卵母細胞成熟YZ因子) 中，表達了大量的活性OMI蛋白(14)。我們發(fā)現(xiàn)mnd2-MSCV細胞用各種刺激劑誘導凋亡時，凋亡細胞的數(shù)量非常低。 進一步講，沒有觀察到可檢測的HAX-1酶切。這和細胞凋亡很旺盛的mnd2-MSCV-OMI細胞相反，并且HAX-1含量和細胞凋亡水平呈反比關系。該試驗清楚地表明了卵母細胞成熟YZ因子單獨決定HAX-1的酶切，在本實驗使用的條件下對于細胞凋亡是必須的。HAX-1的亞細胞位置取決于細胞形狀(21， 30)，并且已經(jīng)有報道說可以存在于線粒體、細胞質(zhì)或質(zhì)膜 (10、21、22、30)中。 我們對細胞亞組分進行了分離操作來研究OMI酶切HAX-1 蛋白的位點。我們發(fā)現(xiàn)HEK293 細胞中的HAX-1蛋白主要存在于線粒體，并且這個位點不隨刺激劑反應的改變而變化。 這暗示著卵母細胞成熟YZ因子靠酶切HAX-1 蛋白來啟動線粒體中的細胞凋亡。這和Z近的研究是一致的，該研究表明卵母細胞成熟YZ因子能誘導用TNF處理的人類神經(jīng)多肽的凋亡而不從線粒體中釋放出來(7)。盡管幾個研究清楚地把HAX-1界定為一種抗凋亡蛋白，它發(fā)揮功能的機理仍然未知。HAX-1 和Bcl-2蛋白家族有序列相似性 (10， 22)。
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- 生物化學翻譯
- To show that HAX-1 degradation is part of the apoptotic process and any involvement Omi may have， we used the ucf-101 inhibitor. ucf-101 is a specific inhibitor of the proteolytic activity of Omi and has been described previously (13). When... To show that HAX-1 degradation is part of the apoptotic process and any involvement Omi may have， we used the ucf-101 inhibitor. ucf-101 is a specific inhibitor of the proteolytic activity of Omi and has been described previously (13). When HK-2 cells were treated with cisplatin in the presence of ucf-101， the percentage of apoptotic cells decreased and the inhibitor significantly blocked HAX-1 degradation. This effect was more pronounced when a higher concentration of the inhibitor was used. To confirm the specificity of the inhibitor in this system and exclude the possibility that another protease rather than Omi is involved in HAX-1 cleavage， we used cell lines derived from mnd2 mice (9). The parent cell line (mnd2-MSCV) derived from mouse embryo fibroblasts has no detectable Omi proteolytic activity (9). The same cell line has been transfected with wild type human Omi cDNA (mnd2-MSCV-Omi) and expresses high levels of active Omi protein (14). We found that in mnd2-MSCV cells， when induced to undergo apoptosis with various stimuli， the number of apoptotic cells was very low. Furthermore， no detectable cleavage of HAX-1 was observed. This is in contrast with the mnd2-MSCV-Omi cells where apoptosis was robust， and HAX-1 levels were inversely proportional to the degree of apoptosis. This experiment clearly shows that Omi is solely responsible for HAX-1 cleavage， which is essential for apoptosis under the conditions used in these experiments. HAX-1 subcellular localization depends on cell type (21， 30) and has been reported to be present in the mitochondria， cytoplasm， or plasma membrane (10， 21， 22， 30). We performed subcellular fractionation to investigate where HAX-1 cleavage by Omi takes place. We found that， in HEK293 cells， HAX-1 was predominantly present in the mitochondria， and this localization did not change in response to apoptotic stimuli. This suggests that Omi can initiate apoptosis in the mitochondria by cleaving HAX-1 protein. This is in accord with a recent study that shows Omi can induce apoptosis in human neutrophils treated with TNF- without being released from the mitochondria (7). Although several studies clearly define HAX-1 as an anti-apoptotic protein， the mechanism of its function is unknown. HAX-1 has sequence similarity to Bcl-2 family of proteins (10， 22). 展開
2007-02-03 21:19:55
522
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- 生物化學考點
- 農(nóng)林類
2011-11-22 08:48:23
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- 生物化學判斷正誤題
- 等摩爾的D-ALa和L-ALa混合液，不能引起偏振光平面的偏轉(zhuǎn)()如果錯誤理由是什么... 等摩爾的D-ALa和 L-ALa混合液，不能引起偏振光平面的偏轉(zhuǎn)() 如果錯誤理由是什么 展開
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- 亞基的生物化學：Biochemistry
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- 生物化學簡答和名詞解釋
- 補考生物化學的的簡答題和名詞解釋誰那里有比較全的請發(fā)下吧！ 馬上就要考試了~~~~~~~ Z好連答案也有
2010-04-22 02:04:19
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- 生物化學有哪些內(nèi)容？
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- 生物化學中PL什么意思
2011-12-26 01:12:54
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- 翻譯翻譯，請高手幫我翻譯一下這個說明
- Followthesysteminstallationinstructionscarefullyandinthespecifiedorder.ThesoftwaremustbeinstalledonthecomputerbeforeconnectingtheUSBcable.2.1FacilitiesRequirementsFacilit... Follow the system installation instructions carefully and in the specified order. The software must be installed on the computer before connecting the USB cable. 2.1 Facilities Requirements Facilities requirements for the alpha-SE system are listed in Table 2-1 and the system dimensions are given in Fig. 2-1. As shown in Fig. 2-2， the alpha-SE tool requires a clear work area of 20 by 18 inches (500 by 460 mm)， excluding the operator computer. 2.2 Unpacking the Hardware Opening the Shipping Container Move the alpha-SE shipping container to the area where the tool will be installed. Open the container and remove the top and side pieces of packing foam. Carefully remove all smaller components from the shipping container， verifying that you received all components， as shown in Fig. 2-3. Finally， remove the alpha-SE ellipsometer and position it on your clear 20” by 18” (510 by 460 mm) workspace. Caution: The alpha-SE ellipsometer without sample chuck weighs approximately 37 lbs. (16 kg.). Please find an assistant to lift the alpha-SE unit out of the shipping carton and on to clear work surface. 展開
2008-06-22 06:30:36
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- 生物化學做一下，謝謝了
- 一、選擇題1、構成輔酶A的維生素有A、生物素B、泛酸C、VB1D、VB22、酶促反應的特點是A、GX性B能觸發(fā)化學反應的進行C、提高反應的活化能D、反應前后酶的質(zhì)量不變3、具有生物活性的全... 一、選擇題 1、構成輔酶A的維生素有 A、生物素 B、泛酸 C、VB1 D、VB2 2、酶促反應的特點是 A、GX性 B能觸發(fā)化學反應的進行 C、提高反應的活化能 D、反應前后酶的質(zhì)量不變 3、具有生物活性的全酶，無輔助因子時 A、有活性 B、無活性 C、無特異性 D、不易失活 4、米氏常數(shù)Km值 A、愈大，酶與底物親和力越高 B、愈小，酶與底物親和力越低 C、愈小，酶與底物親和力越大 D、大小與酶的濃度有關 5、酶原激活過程中，通常使酶原分子中 斷裂 A、氫鍵 B、疏水鍵 C、離子鍵 D、肽鍵 6、酶促反應速度與下列因素成正比的是 A、溫度 B、PH值 C、酶濃度 D、底物濃度 7、缺乏維生素C將導致 A、壞血病 B、夜盲癥 C、貧血 D、瘌皮病 8、核苷酸合成時，需一碳基團，轉(zhuǎn)移一碳基團的輔酶是 A、四氫葉酸 B、NAD C、TPP D、生物素 9、有關同工酶的描述，其中不正確 A、來源可以不同 B、理化性質(zhì)相同 C、催化反應相同 D、分子量可以不同 10、酶的競爭性YZ特點是 A、YZ劑與酶的活性ZX結構相似 B、YZ作用的強弱與YZ劑濃度的大小無關 C、YZ劑濃度不受底物濃度的影響 D、YZ與酶作用的底物結構相似 11、缺乏后，會導致腳氣病的維生素是 A、VB1 B、VB2 C、VC D、VPP 12、下列維生素中參與轉(zhuǎn)氨基的作用的 A、硫胺素 B、尼克酸 C、核黃素 D、磷酸吡哆醛 13、酶催化作用對能量的影響在于 A、增加產(chǎn)物能量水平 B、降低活化能 C、降低反應物能量水平 D、降低反應在自由能 14、下面關于蛋白酶的敘述正確的是 A、所有酶都是蛋白質(zhì) B、所有的酶都含有輔基或輔酶 C、都只能在體內(nèi)起催化作用 D、都有立體異構專一性 15、酶的活性ZX是指 A、酶分子上含有必需基團的肽段 B、酶分子與底物結合部位 C、酶分子與輔酶結合的部位 D、酶分子發(fā)揮催化作用的關鍵性結構區(qū) 二、填空題 1．酶催化的機理是降低反應的 ，不改變反應的____________。 2．酶的特異性包括__________特異性，____________特異性與立體異構特異性。 3．酶活性ZX內(nèi)的必需基團分為__________和__________。 三、名詞解釋 1、米氏常數(shù) 2、同功酶 3、酶原 4、酶活性ZX 四、問答題 1、簡述酶作為生物催化劑下一般化學催化劑的共性及個性。 2、簡述酶的競爭性YZ作用的特點。 展開
2009-05-01 00:02:25
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- 生物化學題目，什么是酶？
- 《大學生物化學》題目：什么是酶？你是如何理解的？（30分）我需要準確答案，請認真回答... 《大學生物化學》題目：什么是酶？你是如何理解的？（30分）我需要準確答案，請認真回答 展開
2012-06-22 05:30:08
553
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- 求生物化學第三版的名詞解釋
2016-01-13 16:41:47
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- 生物化學DNA的生物合成
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- 生物化學 里面的CE是什么
2010-10-29 21:52:42
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- 求翻譯。。。。。。。。。。。
- During the preparation of the nano-products， these nano-units， such as nanoparticles， nanoclusters， nanowires and nanorods， can also self-assemble into the novel structural aggregates by several routes， including electron irradiation deposi... During the preparation of the nano-products， these nano-units， such as nanoparticles， nanoclusters， nanowires and nanorods， can also self-assemble into the novel structural aggregates by several routes， including electron irradiation deposition [19]， chemical vapor deposition [20]， laser vaporization-condensation [21]， charge transferring [22]， an organic reagent-assisted method [23]， solution-liquid-solid method [24] and catalytic vapor-liquid-solid growth [25]. With these routes， various nanoscale or microscale aggregates can demonstrate novel architectures， including tree-like， web-like， spherical， nanowire-like， network and fishbone-like aggregates. As a well-known method for producing the nanocapsules， however， arc-discharge has been rarely used to synthesize the aggregates self-assembled by the nanocapsules prepared simultaneously in arc-discharge. Nevertheless， it is possible that the arc-discharge can be developed into a new way to synthesize the aggregates. In the present work， we utilized arc-discharge technique with modified strategies， involving changing the hydrogen pressure， introducing gadolinium - aluminum alloy ingot as the anode and adjusting the elements percent of the anode according to their evaporation pressure， to synthesize a new type of nanocapsules， with intermetallic compound GdAl2 as core and amorphous Al2O3 as shell， which enlarge the family of the magnetic nanocapsules. At the same time， the regularly aligned three-dimensional macro-aggregates self-assembled by the nanocapsules without any template and catalyst were simultaneously synthesized in arc-discharge process. 展開
2008-06-09 10:41:10
400
1
- 機械翻譯!!
- 13.本系列儀器采用電流、電壓雙組取樣并經(jīng)單片處理后顯示，其讀數(shù)直觀、準確。由于儀器采用了負載四線制取樣，從面消除了負載導線電阻對電顯示的影響。電路的電壓限幅，使得實驗更加安全，可靠。 16.采用古埃法（gu-ai method）研究分子結構，測量順磁和逆... 13.本系列儀器采用電流、電壓雙組取樣并經(jīng)單片處理后顯示，其讀數(shù)直觀、準確。由于儀器采用了負載四線制取樣，從面消除了負載導線電阻對電顯示的影響。電路的電壓限幅，使得實驗更加安全，可靠。 16.采用古埃法（gu-ai method）研究分子結構，測量順磁和逆磁磁化率。主要結構有：電磁鐵和恒流電源、數(shù)字式高斯計（霍爾效應）、安培計和伏特計、配有照明系統(tǒng)的控制盤。系統(tǒng)采用了PID電子調(diào)節(jié)，全數(shù)字電源（0~10A無級調(diào)節(jié)），無需水冷卻，使得儀器動礦層運行更加穩(wěn)定可靠，防止因操作不當而造成儀器損壞。 34. 本儀器由光學系統(tǒng)和信號處理系統(tǒng)兩部分組成，它根據(jù)光拍頻原理設計，通過光電轉(zhuǎn)換檢測，在普通示波器上同時觀察和比較兩束光的波形和相位，測量光程差和位相差，求得光速。 采用新的分頻、觸發(fā)措施，能在示波器上觀察到精確、清晰的波形。 35.本裝置用霍爾效應的原理測量螺線管軸向磁場強度分布。能判斷半導體載流子的符號，移開螺線管，可做共軛線圈實驗。 此裝置由測定儀和專用電源兩部分組成，實驗儀上裝有螺線管、霍爾元件、二維移動標尺及IM，IH，VH轉(zhuǎn)換開關。專用電源提供霍爾元件工作電流IH，螺線管勵磁電流IM以及對霍爾電壓VH的測量。電流和電壓的測量均采用3 1/2位數(shù)顯表，測量精度高。 翻出來后我再給分!一定會追加分!Z少50分!! 展開
2007-03-25 21:10:45
535
1
- 幫忙翻譯
- AttachingtheSampleChuckYouwillneeda#2Phillipsscrewdriverforthisstep.FollowingthedetailsshowninFig.2-4，installthesamplechuckbyfirstaligningthepinsonthebottomofthesamplechu... Attaching the Sample Chuck You will need a #2 Phillips screwdriver for this step. Following the details shown in Fig. 2-4， install the sample chuck by first aligning the pins on the bottom of the sample chuck with the receptacles on the alpha- SE base. Then tighten the upper two captive thumb screws. Next， use the Phillips screwdriver to tighten the lower two captive screws. Don’t over tighten the screws! It will make it difficult to remove them in the future; just ensure that the screws are snug. Finally， connect the vacuum line from the sample chuck to the vacuum fitting on the alpha-SE base. Releasing the Z-stage Shipping Lock To access the Z-stage shipping lock， first loosen the captive screw on the lamp/shipping lock access door， then open the access door by rotating 180°， as shown in Fig. 2-5. To release the Z-stage shipping lock， stand in front of the ellipsometer and use your left hand to balance the weight of the Z-stage (you will feel it lift up slightly). It will be difficult to release the shipping lock if you apply too much or not enough upward force. Next， use your right hand to move the shipping lock to the operating position (to the right， see Fig. 2-6). If the lock is hard to move， you can use a tool to gain more leverage. The shipping lock will move about 1/3” [8mm] to the right. Checking the Lamp Check that the QTH lamp in fully seated in the lamp housing. The lamp is located behind the actuator screw (see Fig. 2-6) and has two white wires protruding from the back of the lamp. Simply push down on the lamp ensuring that the lamp is fully seated in the lamp housing. Rotate the lamp/shipping lock access door to the closed position and hand tighten the captive screw. 拒絕翻譯軟件，翻譯軟件我自己也會用 不是用翻譯軟件我就看不懂，只是，上來找人翻譯就是希望翻譯出比較容易看懂，不需要自己對照就可以看的說明書，如果用翻譯軟件，根本就詞不達意，還是要自己對著原文件核實 既然用了那么多積分，就希望有相當?shù)某晒?，如果用翻譯軟件混積分，那就是人品問題了 還有，某些人不要不懂亂說混積分 展開
2008-06-22 15:11:54
651
5
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