国产一区内射最近更新_99香蕉国产精品偷在线观看_国产六月婷婷爱在线观看_国产午夜大地久久_无码内射中文字幕岛国片

芬蘭Kibron專注表面張力儀測量技術(shù),快速精準測量動靜態(tài)表面張力

熱線:021-66110810,56056830,66110819,66110690,13564362870 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(lián)合大學.jpg

聯(lián)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(jié)論、致謝!

來源:上海謂載 瀏覽 1353 次 發(fā)布時間:2021-10-20


結(jié)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(guān)的脂質(zhì)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(zhì)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(shè)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(zhì)體)的作用。 脂質(zhì)體被證明是 與 LDL 一樣有效地防止 BSP 蛋白插入 磷脂層。 發(fā)現(xiàn) LDL 和 脂質(zhì)體:0.16–0.17 mg 磷脂酰膽堿/mg BSP。 我們不 還知道脂質(zhì)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(zhì)。 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(zhì),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(xiàn) 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(shù)據(jù)


與本文相關(guān)的補充數(shù)據(jù)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(jié)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(jié)論、致謝!

狼人av在线免费观看| 男女做爰真人视频直播| 国产69精品久久久久久久| 国外黄色大片久久久免费| 欧美牲交a免费| 国产亚洲精品aaaa片app| 亚洲综合久久成人a片红豆| 亚洲精品美女久久久久9999| 国产99久久精品一区二区| 国产一级三级视频在线| 亚洲国产成人久久一区| 在线A级毛片无码免费真人| 亚洲夜夜性无码| 国产成人亚洲综合无码| 无码国产色欲xxxxx视频| 色欲网天天无码av| 亚洲av无码一区二区二三区软件| 老妇高潮潮喷到猛进猛出| 亚洲中文字幕在线观看| 国产av一区二区三区天堂综合网 | 亚洲国产精品一区二区第四页| 国产一区二区福利视频| 午夜内射中出视频| 有码中文字幕一区三区| 国产电影一区二区三区| aa片在线观看视频在线播放| 黑人巨大精品欧美| 怀孕挺大肚子疯狂高潮av毛片| 亚洲狠狠婷婷综合久久久久图片| 精国产品一区二区三区a片| 久久www免费人成精品| 亚洲综合欧美在线一区在线播放| 亚洲中文字幕无码爆乳av| 99国产精品国产精品九九| 成年女人毛片免费视频| 色综合99久久久无码国产精品| 国产精品自拍在线视频| 日韩人妻精品无码一区二区三区| 无码粉嫩虎白一线天在线观看 | 爱久久av一区二区三区| 国产免费午夜福利在线播放11|