日韩欧美成人午夜,天天色综合成人网,岛国精品在线,噜噜噜噜噜在线视频,高清在线观看av,成人毛片免费,成人黄色小视频,亚洲免费高清,国产精品每日更新,91精品国产综合久久精品性色

芬蘭Kibron專注表面張力儀測量技術,快速精準測量動靜態表面張力

熱線:021-66110810,66110819,66110690,13564362870 Email: info@vizai.cn

合作客戶/

拜耳公司.jpg

拜耳公司

同濟大學

同濟大學

聯合大學.jpg

聯合大學

寶潔公司

美國保潔

強生=

美國強生

瑞士羅氏

瑞士羅氏

當前位置首頁 > 新聞中心

應用不同組裝的磷脂酰膽堿對牛精漿蛋白的隔離——結論、致謝!

來源:上海謂載 瀏覽 1861 次 發布時間:2021-10-20


結論


首先,表面張力測量證明牛精漿具有非常好的表面活性,這可能與 BSP 蛋白。 二、朗繆爾薄膜法 先前被證明是相關的脂質單層模型 公牛精子的外細胞膜 [35],有助于表征 BSP 蛋白對脂質膜的親和力。 BSP 蛋白是 能夠到達被磷脂覆蓋的牛精子細胞表面,這要歸功于它們與磷脂酰膽堿和 它們自身的表面活性。 我們的假設是,由于它們自己的表面,它們首先穿透精子的外葉 活動然后他們留在那里因為與 磷脂酰膽堿。 最后,Langmuir 薄膜法也得到了 用于篩選已知的 BSP 蛋白螯合劑(如 LDL 和脂質體)的作用。 脂質體被證明是 與 LDL 一樣有效地防止 BSP 蛋白插入 磷脂層。 發現 LDL 和 脂質體:0.16–0.17 mg 磷脂酰膽堿/mg BSP。 我們不 還知道脂質體在 冷凍保存的時間尺度有一些生物學后果。 需要進一步的研究來分析每個的表面特性 BSP 蛋白及其對膜的作用。 此外,可以測試朗繆爾薄膜以檢測 BSP 對膜的親和力隨溫度的變化 [20]。 最后,朗繆爾薄膜法是一種 用于鑒定新的螯合劑的強大篩選方法 BSP 蛋白質。 這種方法可以適用于其他動物物種。


致謝


作者要感謝 IMV Technologies(法國) 其財政支持,Gérard Chatagnon 的量化 精漿中的蛋白質,凝膠電泳的 Véronique Solé,英語校正的 Maureen Collobert 和 Alain Sire 和 Patrice Papineau 的概念和實現 手套箱允許在受控的情況下使用 Langmuir 槽進行工作 大氣層。


附錄 A. 補充數據


與本文相關的補充數據可以在 在線版本,見 http://dx.doi.org/10.1016/j.colsurfb.2015.11。 034.


參考


[1] F. Ardon, S.S. Suarez, Cryopreservation increases coating of bull sperm by seminal plasma binder of sperm proteins BSP1, BSP3, and BSP5, Reproduction 146 (2013) 111–117, http://dx.doi.org/10.1530/rep-12-0468.


[2] P. Manjunath, J. Lefebvre, P.S. Jois, J. Fan, M.W. Wright, New nomenclature for mammalian BSP genes, Biol. Reprod. 80 (2009) 394–397, http://dx.doi.org/10. 1095/biolreprod.108.074088.


[3] V. Nauc, P. Manjunath, Radioimmunoassays for bull seminal plasma proteins (BSP-A1/-A2, BSP-A3, and BSP-30-Kilodaltons), and their quantification in seminal plasma and sperm, Biol. Reprod. 63 (2000) 1058–1066, http://dx.doi. org/10.1095/biolreprod63.4.1058.


[4] F.S. Esch, N.C. Ling, P. B?hlen, S.Y. Ying, R. Guillemin, Primary structure of PDC-109, a major protein constituent of bovine seminal plasma, Biochem. Biophys. Res. Commun. 113 (1983) 861–867, http://dx.doi.org/10.1016/0006- 291x(83)91078-1.


[5] N.G. Seidah, P. Manjunath, J. Rochemont, M.R. Sairam, M. Chrétien, Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin, Biochem. J. 243 (1987) 195–203.


[6] J.J. Calvete, K. Mann, L. Sanz, M. Raida, E. T?pfer-Petersen, The primary structure of BSP-30K, a major lipid-, gelatin-, and heparin-binding glycoprotein of bovine seminal plasma, FEBS Lett. 399 (1996) 147–152, http:// dx.doi.org/10.1016/s0014-5793(96)1310-5.


[7] D. Salois, M. Ménard, Y. Paquette, P. Manjunath, Complementary deoxyribonucleic acid cloning and tissue expression of BSP-A3 and BSP-30-kDa: phosphatidylcholine and heparin-binding proteins of bovine seminal plasma, Biol. Reprod. 61 (1999) 288–297, http://dx.doi.org/10.1095/ biolreprod61.1.288.


[8] P. Manjunath, M.R. Sairam, J. Uma, Purification of four gelatin-binding proteins from bovine seminal plasma by affinity chromatography, Biosci. Rep. 7 (1987) 231–238, http://dx.doi.org/10.1007/bf01124794.


[9] L. Desnoyers, P. Manjunath, Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid, J. Biol. Chem. 267 (1992) 10149–10155.


[10] L. Desnoyers, P. Manjunath, Interaction of a novel class of phospholipid-binding proteins of bovine seminal fluid with different affinity matrices, Arch. Biochem. Biophys. 305 (1993) 341–349, http://dx.doi.org/10. 1006/abbi.1993.1431.


[11] P. Müller, K.-R. Erlemann, K. Müller, J.J. Calvete, E. T?pfer-Petersen, K. Marienfeld, et al., Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles, Eur. Biophys. J. 27 (1998) 33–41, http://dx.doi.org/10.1007/s002490050108.


[12] P. Manjunath, I. Thérien, Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation, J. Reprod. Immunol. 53 (2002) 109–119, http://dx.doi.org/10. 1016/s0165-0378(01)98-5.


[13] M. Ramakrishnan, V. Anbazhagan, T.V. Pratap, D. Marsh, M.J. Swamy, Membrane insertion and lipid-protein interactions of bovine seminal plasma protein PDC-109 investigated by spin-label electron spin resonance spectroscopy, Biophys. J. 81 (2001) 2215–2225, http://dx.doi.org/10.1016/ S0006-3495(01)75869-9.


[14] D.A. Wah, C. Fernández-Tornero, L. Sanz, A. Romero, J.J. Calvete, Sperm coating mechanism from the 1.8? crystal structure of PDC-109-phosphorylcholine complex, Structure 10 (2002) 505–514, http://dx.doi.org/10.1016/s0969- 2126(02)751-7.


[15] P. Manjunath, M.R. Sairam, Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma, Biochem. J. 241 (1987) 685–692.


[16] R.S. Damai, V. Anbazhagan, K.B. Rao, M.J. Swamy, Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes, Biochim. Biophys. Acta: Proteins Proteomics. 1794 (2009) 1725–1733, http://dx.doi.org/10.1016/j. bbapap.2009.08.010.


[17] A. Bergeron, M.-H. Crête, Y. Brindle, P. Manjunath, Low-density lipoprotein fraction from hen's egg yolk decreases the binding of the major proteins of bovine seminal plasma to sperm and prevents lipid efflux from the sperm membrane, Biol. Reprod. 70 (2004) 708–717, http://dx.doi.org/10.1095/ biolreprod.103.022996.


[18] A. Tannert, E. T?pfer-Petersen, A. Herrmann, K. Müller, P. Müller, The lipid composition modulates the influence of the bovine seminal plasma protein PDC-109 on membrane stability, Biochemistry 46 (2007) 11621–11629, http://dx.doi.org/10.1021/bi7011299.


[19] I. Thérien, G. Bleau, P. Manjunath, Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin, Biol. Reprod. 52 (1995) 1372–1379, http://dx.doi.org/10.1095/biolreprod52.6. 1372.


[20] D. Lassiseraye, L. Courtemanche, A. Bergeron, P. Manjunath, M. Lafleur, Binding of bovine seminal plasma protein BSP-A1/-A2 to model membranes: lipid specificity and effect of the temperature, Biochim. Biophys. Acta: Biomembr. 1778 (2008) 502–513, http://dx.doi.org/10.1016/j.bbamem.2007. 10.025.


[21] I. Thérien, R. Moreau, P. Manjunath, Major proteins of bovine seminal plasma and high-density lipoprotein induce cholesterol efflux from epididymal sperm, Biol. Reprod. 59 (1998) 768–776, http://dx.doi.org/10.1095/ biolreprod59.4.768.


[22] I. Thérien, R. Moreau, P. Manjunath, Bovine seminal plasma phospholipid-binding proteins stimulate phospholipid efflux from epididymal sperm, Biol. Reprod. 61 (1999) 590–598, http://dx.doi.org/10. 1095/biolreprod61.3.590.


[23] A. Bergeron, P. Manjunath, New insights towards understanding the mechanisms of sperm protection by egg yolk and milk, Mol. Reprod. Dev. 73 (2006) 1338–1344, http://dx.doi.org/10.1002/mrd.20565.


[24] P. Müller, A. Greube, E. T?pfer-Petersen, A. Herrmann, Influence of the bovine seminal plasma protein PDC-109 on cholesterol in the presence of phospholipids, Eur. Biophys. J. 31 (2002) 438–447, http://dx.doi.org/10.1007/ s00249-002-0234-2.


[25] T.S. Witte, S. Sch?fer-Somi, Involvement of cholesterol, calcium and progesterone in the induction of capacitation and acrosome reaction of mammalian spermatozoa, Anim. Reprod. Sci. 102 (2007) 181–193, http://dx. doi.org/10.1016/j.anireprosci.2007.07.007.


[26] P. Manjunath, V. Nauc, A. Bergeron, M. Ménard, Major proteins of bovine seminal plasma bind to the low-density lipoprotein fraction of hen's egg yolk, Biol. Reprod. 67 (2002) 1250–1258, http://dx.doi.org/10.1095/biolreprod67.4. 1250.


[27] M.-F. Lusignan, A. Bergeron, M. Lafleur, P. Manjunath, The major proteins of bovine seminal plasma interact with caseins and whey proteins of milk extender, Biol. Reprod. 85 (2011) 457–464, http://dx.doi.org/10.1095/ biolreprod.110.089961.


[28] L. Amirat, D. Tainturier, L. Jeanneau, C. Thorin, O. Gerard, J.L. Courtens, et al., Bull semen in vitro fertility after cryopreservation using egg yolk LDL: a comparison with Optidyl®, a commercial egg yolk extender, Theriogenology 61 (2004) 895–907.


[29] J.A. Foulkes, D.L. Stewart, Fertility of dairy-cattle after artificial-insemination with semen frozen in a lipoprotein diluent, J. Reprod. Fertil. 51 (1977) 175–177.


[30] J.A. Foulkes, Separation of lipoproteins from egg-yolk and their effect on motility and integrity of bovine spermatozoa, J. Reprod. Fertil. 49 (1977) 277–284.


[31] M. Moussa, V. Martinet, A. Trimeche, D. Tainturier, M. Anton, Low density lipoproteins extracted from hen egg yolk by an easy method: cryoprotective effect on frozen-thawed bull semen, Theriogenology 57 (2002) 1695–1706.


[32] M.M. Pace, E.F. Graham, Components in egg yolk which protect bovine spermatozoa during freezing, J. Anim. Sci. 39 (1974) 1144–1149.


[33] M. Anton, V. Martinet, M. Dalgalarrondo, V. Beaumal, E. David-Briand, H. Rabesona, Chemical and structural characterisation of low-density lipoproteins purified from hen egg yolk, Food Chem. 83 (2003) 175–183, http://dx.doi.org/10.1016/s0308-8146(03)60-8.


[34] M.-F. Lusignan, P. Manjunath, M. Lafleur, Thermodynamics of the interaction between bovine binder of sperm BSP1 and low-density lipoprotein from hen's egg yolk, Thermochim. Acta 516 (2011) 88–90, http://dx.doi.org/10.1016/j. tca.2011.01.003.


[35] J. Le Guillou, M.H. Ropers, C. Gaillard, E. David-Briand, S. Desherces, E. Schmitt, et al., Organization of lipids in the artificial outer membrane of bull spermatozoa reconstructed at the air–water interface, Colloids Surfaces B: Biointerfaces 108 (2013) 246–254, http://dx.doi.org/10.1016/j.colsurfb.2013. 02.040.


[36] A. Seelig, Local anesthetics and pressure: a comparison of dibucaine binding to lipid monolayers and bilayers, Biochim. Biophys. Acta 899 (1987) 196–204, http://dx.doi.org/10.1016/0005-2736(87)90400-7.


[37] P. Manjunath, L. Chandonnet, E. Leblond, L. Desnoyers, Major proteins of bovine seminal vesicles bind to spermatozoa, Biol. Reprod. 50 (1994) 27–37, http://dx.doi.org/10.1095/biolreprod50.1.27.


[38] A. Berthold, H. Schubert, N. Brandes, L. Kroh, R. Miller, Behaviour of BSA and of BSA-derivatives at the air/water interface, Colloids Surfaces A: Physicochem. Eng. Aspects 301 (2007) 16–22, http://dx.doi.org/10.1016/j.colsurfa.2006.11. 054.


[39] V.S. Alahverdjieva, D.O. Grigoriev, J.K. Ferri, V.B. Fainerman, E.V. Aksenenko, M.E. Leser, et al., Adsorption behaviour of hen egg-white lysozyme at the air/water interface, Colloids Surfaces A: Physicochem. Eng. Aspects 323 (2008) 167–174, http://dx.doi.org/10.1016/j.colsurfa.2007.12.031.


[40] H.M. Mansour, G. Zografi, Relationships between equilibrium spreading pressure and phase equilibria of phospholipid bilayers and monolayers at the air–water interface, Langmuir 23 (2007) 3809–3819, http://dx.doi.org/10. 1021/la063053o.


[41] L.E. Palacios, T. Wang, Egg-yolk lipid fractionation and lecithin characterization, JAOCS, J. Am. Oil Chem. Soc. 82 (2005) 571–578, http://dx. doi.org/10.1007/s11746-005-1111-4.


[42] C.J. Thomas, V. Anbazhagan, M. Ramakrishnan, N. Sultan, I. Surolia, M.J. Swamy, Mechanism of membrane binding by the bovine seminal plasma protein, PDC-109: a surface plasmon resonance study, Biophys. J. 84 (2003) 3037–3044, http://dx.doi.org/10.1016/s0006-3495(03)70029-0.


[43] U. Dahmen-Levison, G. Brezesinski, H. M?hwald, Specific adsorption of PLA2 at monolayers, Thin Solid Films 327–329 (1998) 616–620, http://dx.doi.org/ 10.1016/s0040-6090(98)725-1.


[44] V. Anbazhagan, R.S. Damai, A. Paul, M.J. Swamy, Interaction of the major protein from bovine seminal plasma, PDC-109 with phospholipid membranes and soluble ligands investigated by fluorescence approaches, Biochim. Biophys. Acta: Proteins Proteomics. 1784 (2008) 891–899, http://dx.doi.org/ 10.1016/j.bbapap.2008.03.002.


[45] V. Anbazhagan, M.J. Swamy, Thermodynamics of phosphorylcholine and lysophosphatidylcholine binding to the major protein of bovine seminal plasma, PDC-109, FEBS Lett. 579 (2005) 2933–2938, http://dx.doi.org/10. 1016/j.febslet.2005.04.046.


[46] P. Manjunath, New insights into the understanding of the mechanism of sperm protection by extender components, Anim. Reprod. 9 (2012) 809–815.


[47] M. Gasset, L. Magdaleno, J.J. Calvete, Biophysical study of the perturbation of model membrane structure caused by seminal plasma protein PDC-109, Arch. Biochem. Biophys. 374 (2000) 241–247, 10.1006/abbi.1999.1593\rS000398619991593X [pii].


[48] A. Greube, K. Müller, E. T?pfer-Petersen, A. Herrmann, P. Müller, Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes, Biochemistry 40 (2001) 8326–8334, http://dx.doi.org/10.1021/ bi010552+.


[49] I. Thérien, S. Soubeyrand, P. Manjunath, Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein, Biol. Reprod. 57 (1997) 1080–1088, http://dx.doi.org/10.1095/biolreprod57.5. 1080.


[50] M. Lafleur, L. Courtemanche, G. Karlsson, K. Edwards, J.L. Schwartz, P. Manjunath, Bovine binder-of-sperm protein BSP1 promotes protrusion and nanotube formation from liposomes, Biochem. Biophys. Res. Commun. 399 (2010) 406–411, http://dx.doi.org/10.1016/j.bbrc.2010.07.088.


應用不同組裝的磷脂酰膽堿對牛精漿蛋白的隔離——摘要、簡介

應用不同組裝的磷脂酰膽堿對牛精漿蛋白的隔離——材料與方法

應用不同組裝的磷脂酰膽堿對牛精漿蛋白的隔離——結果與討論

應用不同組裝的磷脂酰膽堿對牛精漿蛋白的隔離——結論、致謝!

欧美国产日韩二区| 婷婷午夜社区一区| 青青草成人在线| 91国产精品91| 国产成人精品综合久久久| 国产suv精品一区二区三区88区| 成人欧美在线| 成视频在线观看免费观看| 国产久一一精品| 午夜在线不卡| av小片在线| 国产美女福利在线观看| 午夜不卡影院| 亚洲一区二区小说| 久久国产精品免费精品3p| 网友自拍一区| 影音先锋日韩精品| 久久激情久久| 成人黄色大片在线观看 | 中文字幕日韩欧美在线| 久久久97精品| 欧美一级大片在线观看| 3344永久| 超碰国产在线| 日本免费一区二区三区四区| 日韩精品中文字幕吗一区二区| 国产欧美一区二区三区米奇| 三上亚洲一区二区| 日韩综合一区二区| 久久五月婷婷丁香社区| 亚洲444eee在线观看| 5858s免费视频成人| 日韩在线观看精品| 国产欧洲精品视频| 91亚洲天堂| baoyu135国产精品免费| 国产伊人精品| 91一区二区在线观看| 婷婷一区二区三区| 日韩精品中文字幕在线观看| 91高清免费在线观看| 一二三中文字幕在线| 午夜国产不卡在线观看视频| 中文欧美在线视频| 欧美激情精品久久久久久久变态| 国产日韩精品在线播放| 日本高清在线观看wwwww色| 黄色综合网址| 欧美freesextv| 国产传媒欧美日韩成人| 亚洲午夜三级在线| 香蕉精品久久| 性国产高清在线观看| 国产一区二区三区| 在线看片欧美| 久久精品视频在线免费观看| 欧美三级视频在线| 久久久www成人免费精品| 成人频在线观看| 不卡av播放| 国产精品99一区二区| 久久久99精品久久| 精品成人a区在线观看| 国产日本欧美一区二区三区| 亚洲福利影院| 国产欧美日韩一级| 亚洲成人av一区二区| 色噜噜狠狠色综合网图区| 91精品免费看| 国产精品高清免费在线观看| 中文字幕一区二区三区在线观看| 精品国产麻豆| 欧美大胆a视频| 国产日韩一级二级三级| 日韩三级成人| 国产精品一久久香蕉国产线看观看| 国产日韩欧美综合| 欧美办公室脚交xxxx| 手机在线电影一区| 中文字幕巨乱亚洲| 亚洲美女av电影| 在线观看国产高清视频| 国产精品一区二区三区av| 麻豆精品一区二区av白丝在线| 91国产免费看| 国产免费一区二区三区香蕉精| 国产精品伦理| 捆绑变态av一区二区三区| 欧美色老头old∨ideo| 国产精品视频网址| 91成人小视频| 成人免费毛片嘿嘿连载视频| 精品三级av在线| 高清色视频在线观看| 久久久免费毛片| 91色|porny| 伊人激情综合网| 国产精品va在线观看视色| 亚洲最新av| 欧美视频在线看| 国产精品女主播| 视频一区在线| 久久久久国产一区二区三区四区| 亚洲男人的天堂在线| 成年人在线看| 午夜日韩电影| 日韩欧美精品在线观看| 国产视频999| 久久综合另类图片小说| 久久精品视频一区| 国精产品一区一区三区有限在线| 伊人成综合网站| 国精品**一区二区三区在线蜜桃| 精品蜜桃在线看| 91美女视频在线| 一级成人国产| 日韩午夜精品电影| 色三级在线观看| 久久精品人人做人人爽电影蜜月| 日韩精品一区二区三区老鸭窝 | 亚洲激情视频在线观看| 超碰在线影院| 日韩影院免费视频| 亚洲国产第一页| 韩国日本一区| 国产精品996| 欧美成人全部免费| 激情视频亚洲| 亚洲综合在线视频| 日本福利小视频| 欧美精品大片| 精品国产一区二区精华| 日本小视频在线免费观看| 国产一区二区三区四区在线观看| 色小说视频一区| 99久久999| 亚洲一级电影视频| 偷拍25位美女撒尿视频在线观看| 亚洲另类黄色| 日韩精品黄色网| 91tv亚洲精品香蕉国产一区| 久久久噜噜噜久噜久久综合| 国产精品99久久久久久久久久久久 | 色视频在线观看免费| 久久精品九九| 久久av在线看| 亚洲影院天堂中文av色| 色婷婷av一区二区三区软件| 成人动漫在线播放| 美女视频黄久久| 欧美黄色小视频| 国模精品一区| 亚洲大胆美女视频| 99riav视频一区二区| 国产精品免费看片| 香蕉视频免费在线| 国产精品亚洲专一区二区三区| 2024亚洲男人天堂| 在线一区免费| 国产一区二区三区在线看| 日本超碰一区二区| 欧美日韩国产首页| 成人线上视频| 精品高清美女精品国产区| 免费观看在线黄色网| 久久久精品影视| 日韩精品123| 99视频国产精品| 久久久久久五月天久久久久久久久| 日日夜夜免费精品| 青青a在线精品免费观看| 午夜精品亚洲| 久久国产天堂福利天堂| 99成人在线视频| 在线观看国产欧美| 日本一本不卡| 精品国产欧美一区二区五十路| 精品国产乱码久久久久久1区2匹| 亚洲国产另类久久精品| 久久久久97| 亚洲人精品午夜在线观看| 国际精品欧美精品| 久久久99免费视频| 亚洲最新色图| 欧美激情视频给我| 在线欧美日韩| 日产精品99久久久久久| 日韩中文字幕区一区有砖一区| 国产不卡精品视男人的天堂| 亚洲尤物精选| 国产精品一区专区欧美日韩| 狠狠狠色丁香婷婷综合久久五月| 国产日韩视频在线观看| 国产a视频精品免费观看| 视频在线91| 欧美极品美女视频| av在线官网| 欧美综合在线视频| 草莓视频一区二区三区| 在线观看欧美日韩|