中国畜牧兽医 ›› 2022, Vol. 49 ›› Issue (12): 4715-4724.doi: 10.16431/j.cnki.1671-7236.2022.12.021
薛丽娥, 曹嘉程, 陈德军, 饶勇勇, 林瑞意, 肖天放, 方绍明
收稿日期:
2022-05-11
出版日期:
2022-12-05
发布日期:
2022-12-01
通讯作者:
方绍明
E-mail:15279156575@163.com
作者简介:
薛丽娥,E-mail:2535288283@qq.com。
基金资助:
XUE Li'e, CAO Jiacheng, CHEN Dejun, RAO Yongyong, LIN Ruiyi, XIAO Tianfang, FANG Shaoming
Received:
2022-05-11
Online:
2022-12-05
Published:
2022-12-01
摘要: 抗冻蛋白(antifreeze proteins,AFPs)是一类能抑制冰晶生长并提高机体抗冻功能的蛋白质。AFPs来源广泛,在动物、植物、细菌、真菌等不同生物体内都存在。目前,研究较多、有望被推广应用于畜牧生产实践的主要是具有热滞活性和抑制冰晶重结晶活性的鱼类AFPs。鱼类AFPs的种类主要包括AFPⅠ、AFPⅡ、AFPⅢ、AFPⅣ和抗冻糖蛋白(AFGP)。尽管不同鱼类AFPs都具有抗冻功能,但是它们的组成和结构差异很大,而且对应的基因在核苷酸序列上几乎没有相似性。鱼类AFPs抗冻机制主要包括吸附-抑制学说、刚体能量学说、包合物锚定学说、亲和相互作用偶联团聚学说等。在人类、鱼类、家畜和小鼠等精液的低温保存中,鱼类AFPs可通过维持细胞膜完整性、抑制冰晶生长及减少DNA损伤等保护精子;在卵母细胞、精原细胞、红细胞及动物胚胎的低温保存中,鱼类AFPs可通过阻止冰晶化及抗氧化功能等改善保存效果。作者主要概述了鱼类AFPs种类及其结构特征和作用机制,总结了鱼类AFPs在精液、卵母细胞、精原细胞、红细胞及胚胎低温保存中的应用进展,以期为鱼类AFPs作为候选抗冻剂应用于种质资源保护和畜牧业生产提供科学依据。
中图分类号:
薛丽娥, 曹嘉程, 陈德军, 饶勇勇, 林瑞意, 肖天放, 方绍明. 鱼类抗冻蛋白在动物精液、细胞、胚胎低温保存中的研究进展[J]. 中国畜牧兽医, 2022, 49(12): 4715-4724.
XUE Li'e, CAO Jiacheng, CHEN Dejun, RAO Yongyong, LIN Ruiyi, XIAO Tianfang, FANG Shaoming. Research Progress on Fish Antifreeze Proteins in Cryopreservation of Animals Semen, Cells and Embryos[J]. China Animal Husbandry & Veterinary Medicine, 2022, 49(12): 4715-4724.
[1] 钟鸣, 蔡继峰, 文继舫.昆虫抗冻蛋白的研究进展[J].生物技术通报, 2010, 10:8-14. ZHONG M, CAI J F, WEN J F.Advances in insect antifreeze protein research[J].Biotechnology Bulletin, 2010, 10:8-14.(in Chinese) [2] 谢秀杰, 贾宗超, 魏群.抗冻蛋白结构与抗冻机制[J].细胞生物学杂志, 2005, 1:5-8. XIE X J, JIA Z C, WEI Q.Antifreeze protein structure and antifreeze mechanism[J].Chinese Journal of Cell Biology, 2005, 1:5-8.(in Chinese) [3] DEVRIES A L, WOHLSCHLAG D E.Freezing resistance in some antarctic fishes[J].Science, 1969, 163(3871):1073-1075. [4] BAR D M, BRASLAVSKY I, DAVIES P L.Ice-binding proteins and their function[J].Annual Review of Biochemistry, 2016, 85:515-542. [5] 李文轲, 马春森.抗冻蛋白特征、作用机理与预测新进展[J].生命科学, 2012, 24(10):1089-1097. LI W K, MA C S.Present properties, mechanism and prediction of antifreeze proteins[J].Chinese Bulletin of Life Sciences, 2012, 24(10):1089-1097.(in Chinese) [6] 胡瑞芹.抗冻蛋白基因ld4提高鱼类抗寒性能的分子机制研究[D].上海:上海海洋大学, 2019. HU R Q.Molecular mechainsm of antifreeze protein gene ld4 improving cold restistance of fish[D].Shanghai:Shanghai Ocean University, 2019.(in Chinese) [7] 张俊芳, 陶筱帆, 韩兵社.南极鱼抗冻蛋白功能和进化及其应用研究进展[J].中国水产科学, 2020, 27(3):355-361. ZHANG J F, TAO X F, HAN B S.Research progress on the function, evolution and application of antifreeze proteins in antarctic fish[J].Journal of Fishery Sciences of China, 2020, 27(3):355-361.(in Chinese) [8] MARSHALL C B, CHAKRABARTTY A, DAVIES P L.Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices[J].Journal of Biological Chemistry, 2005, 280(18):17920-17929. [9] 王勇杰.抗冷冻蛋白Ⅲ对玻璃化冷冻猪卵母细胞保护作用的研究[D].南宁:广西大学, 2020. WANG Y J, Protective effect of antifreeze protein Ⅲ on vitrified frozen porcine oocytes[D].Nanning:Guangxi University, 2020.(in Chinese) [10] MIURA K, OHGIYA S, HOSHINO T, et al.NMR analysis of type Ⅲ antifreeze protein intramolecular dimer.Structural basis for enhanced activity[J].Journal of Biological Chemistry, 2001, 276(2):1304-1310. [11] DENG G, ANDREWS D W, LAURSEN R A.Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin myoxocephalus octodecimspinosis[J].FEBS Letters, 1997, 402(1):17-20. [12] BURCHAM T S, OSUGA D T, RAO B N, et al.Purification and primary sequences of the major arginine-containing antifreeze glycopeptides from the fish Eleginus gracilis[J].Journal of Biological Chemistry, 1986, 261(14):6384-6389. [13] GONG Z, KING M J, FLETCHER G L, et al.The antifreeze protein genes of the winter flounder, pleuronectus americanus, are differentially regulated in liver and non-liver tissues[J].Biochemical and Biophysical Research Communications, 1995, 206(1):387-392. [14] GRAETHER S P, SLUPSKY C M, DAVIES P L, et al.Structure of type Ⅰ antifreeze protein and mutants in supercooled water[J].Biophysical Journal, 2001, 81(3):1677-1683. [15] BARRETT J.Thermal hysteresis proteins[J].International Journal of Biochemistry Cell Biology, 2001, 33(2):105-117. [16] NISHIMIYA Y, KONDO H, TAKAMICHI M, et al.Crystal structure and mutational analysis of Ca2+-independent type Ⅱ antifreeze protein from longsnout poacher, Brachyopsis rostratus[J].Journal of Molecular Biology, 2008, 382(3):734-746. [17] DENG C, CHENG C H, YE H, et al.Evolution of an antifreeze protein by neofunctionalization under escape from adaptive conflict[J].Proceedings of the National Academy of Sciences of the United States of America, 2010, 107(50):21593-21598. [18] HARDING M M, ANDERBERG P I, HAYMET A D.‘Antifreeze’ glycoproteins from polar fish[J].European Journal Biochemistry, 2003, 270(7):1381-1392. [19] YEH Y, FEENEY R E.Antifreeze proteins:Structures and mechanisms of function[J].Chemical Reviews, 1996, 96(2):601-618. [20] KRISTIANSEN E, ZACHARIASSEN K E.The mechanism by which fish antifreeze proteins cause thermal hysteresis[J].Cryobiology, 2005, 51(3):262-280. [21] YANG D S, SAX M, CHAKRABARTTY A, et al.Crystal structure of an antifreeze polypeptide and its mechanistic implications[J].Nature, 1988, 333(6170):232-237. [22] DEVRIES A L.Antifreeze peptides and glycopeptides in cold-water fishes[J].Annual Review of Biochemistry, 1983, 45:245-260. [23] KNIGHT C A.Adding to the antifreeze agenda[J].Nature (London), 2000, 406(6793):249-251. [24] 樊绍刚, 张党权, 邓顺阳, 等.抗冻蛋白和冰核蛋白对植物抗冻性能的作用机制[J].经济林研究, 2009, 27(2):125-130. FAN S G, ZHANG D Q, DENG S Y, et al.Mechanism of antifreeze protein and ice nucleoproteinon plant antifreeze activity[J].Nnowood Forest Research, 2009, 27(2):125-130.(in Chinese) [25] WANG J H.A comprehensive evaluation of the effects and mechanisms of antifreeze proteins during low-temperature preservation[J].Cryobiology, 2000, 41(1):1-9. [26] RAYMOND J A, DEVRIES A L.Adsorption inhibition as a mechanism of freezing resistance in polar fishes[J].Proceedings of the National Academy of Sciences of the United States of America, 1977, 74(6):2589-2593. [27] DUMAN J G.Animal ice-binding (antifreeze) proteins and glycolipids:An overview with emphasis on physiological function[J].Journal of Experimental Biology, 2015, 218(Pt 12):1846-1855. [28] VENKETESH S, DAYANANDA C.Properties, potentials, and prospects of antifreeze proteins[J].Critical Reviews Biotechnology, 2008, 28(1):57-82. [29] 冯从经, 陆剑锋, 吕文静, 等.抗冻蛋白研究进展[J].江苏农业学报, 2007, 5:481-486. FENG C J, LU J F, LYU W J, et al.Advances in antifreeze proteins research[J].Jangsu Journal of Agriculture Sceience, 2007, 5:481-486.(in Chinese) [30] KNIGHT C A, DRIGGERS E, DEVRIES A L.Adsorption to ice of fish antifreeze glycopeptides 7 and 8[J].Biophysical Journal, 1993, 64(1):252-259. [31] 彭淑红, 姚鹏程, 徐宁迎.抗冻蛋白的特性和作用机制[J].生理科学进展, 2003, 3:238-240. PENG S H, YAO P C, XU N Y.Properties and mechanism of action of antifreeze proteins[J]. Advances in Physiological Science, 2003, 3:238-240.(in Chinese) [32] GARNHAM C P, CAMPBELL R L, DAVIES P L.Anchored clathrate waters bind antifreeze proteins to ice[J].Proceedings of the National Academy of Sciences of the United States of America, 2011, 108(18):7363-7367. [33] 陈闯, 姚骏, 王麒琳, 等.抗冻蛋白的研究现状及其应用[J].食品研究与开发, 2016, 37(12):199-201. CHEN C, YAO J, WANG Q L, et al.The research status and application of antifreeze proteins[J].Food Research and Development, 2016, 37(12):199-201.(in Chinese) [34] KNIGHT C A, DEVRIES A L.Ice growth in supercooled solutions of a biological "antifreeze", AFGP 1-5:An explanation in terms of adsorption rate for the concentration dependence of the freezing point[J].Physical Chemistry Chemical Physics, 2009, 11(27):5749-5761. [35] MARSHALL C B, DALEY M E, GRAHAM L A, et al.Identification of the ice-binding face of antifreeze protein from tenebrio molitor[J].FEBS Letters, 2002, 529(2-3):261-267. [36] 钱卓蕾, 王君晖, 边红武, 等.抗冻蛋白在超低温保存中作用机制的新模型[J].细胞生物学杂志, 2002, 4:224-226. QIAN Z L, WANG J H, BIAN H W, et al.A new model for the mechanism of action of antifreeze proteins in cryopreservation[J].Journal of Cell Biology, 2002, 4:224-226.(in Chinese) [37] MEHDIPOUR M, DAGHIGH-KIA H, NAJAFI A, et al.Type Ⅲ antifreeze protein (AFPⅢ) improves the post-thaw quality and in vivo fertility of rooster spermatozoa[J].Poultry Science, 2021, 100(8):101291. [38] BEIRAO J, ZILLI L, VILELLA S, et al.Improving sperm cryopreservation with antifreeze proteins:Effect on gilthead seabream (Sparus aurata) plasma membrane lipids[J].Biology of Reproduction, 2012, 86(2):59. [39] SAEED Z, BITA E, NAHID M, et al.Evaluation of antifreeze protein Ⅲ for cryopreservation of human sperm[J].Cryobiology, 2018, 85:125-126. [40] YOUNIS A I, ROOKS B, KHAN S, et al.The effects of antifreeze peptide Ⅲ (AFP) and insulin transferrin selenium (ITS) on cryopreservation of chimpanzee (Pan troglodytes) spermatozoa[J].Journal of Andrology, 1998, 19(2):207-214. [41] QADEER S, KHAN M A, ANSARI M S, et al.Evaluation of antifreeze protein Ⅲ for cryopreservation of Nili-Ravi (Bubalus bubalis) buffalo bull sperm[J].Animmal Reproduction Science, 2014, 148(1-2):26-31. [42] 权国波, 吴国权, 吕春荣, 等.抗冻蛋白对山羊精子结构和功能的冷冻保护作用分析[A].2017年全国养羊生产与学术研讨会暨养羊学分会第七次全国会员代表大会[C].2017. QUAN G B, WU G Q, LYU C R, et al.Analysis of cryoprotective effect of antifreeze protein on structure and function of goat sperm[A].2017 National Symposium on Sheep Production and Academic Conference and the Seventh National Member Congress of Sheep Science Branch[C].2017.(in Chinese) [43] CORREIA L F L, ESPÍRITOSANTO C G, BRAGA R F, et al.Addition of antifreeze protein type Ⅰ or Ⅲ to extenders for ram sperm cryopreservation[J].Cryobiology, 2021, 98:194-200. [44] ANNA S, MARIOLA D, MO X, et al.Seminal plasma transferrin effects on cryopreserved common carp cyprinus carpio sperm and comparison with bovine serum albumin and antifreeze proteins[J].Animal Reproduction Science, 2019, 204:125-130. [45] XIN M, STERBA J, SHALIUTINA-KOLESOVA A, et al.Protective role of antifreeze proteins on sterlet (Acipenser ruthenus) sperm during cryopreservation[J].Fish Physiology and Biochemistry, 2018, 44(6):1527-1533. [46] MIAOMIAO X, VLADIMÍRA T, MAREK R, et al.Effects of antifreeze proteins on cryopreserved sterlet (Acipenser ruthenus) sperm motility variables and fertilization capacity[J].Animal Reproduction Science, 2018, 196:143-149. [47] KIM D.Evaluation of antifreeze proteins on miniature pig sperm viability, DNA damage, and acrosome status during cryopreservation[J].Journal of Animal Reproduction and Biotechnology, 2016, 31(4):128576. [48] KOSHIMOTO C, MAZUR P.Effects of warming rate, temperature, and antifreeze proteins on the survival of mouse spermatozoa frozen at an optimal rate[J].Cryobiology, 2002, 45(1):49-59. [49] KAZUTOSHI N, MAI T, YUSUKE S, et al.Effects of type Ⅲ antifreeze protein on sperm and embryo cryopreservation in rabbit[J].Cryobiology, 2014, 69(1):22-25. [50] MEHDIPOUR M, DAGHIGH-KIA H, NAJAFI A, et al.Type Ⅲ antifreeze protein (AFP) improves the post-thaw quality and in vivo fertility of rooster spermatozoa[J].Poultry Science, 2021, 100(8):101291. [51] 周健.抗冻蛋白对内蒙古绒山羊精液保存的影响[D].呼和浩特:内蒙古农业大学, 2020. ZHOU J.Effect of antifreeze protien on semen preservation of Inner Mongolia cashmere goat[D].Hohhot:Inner Mongolia Agrichltural University, 2020.(in Chinese) [52] HOSSEN S, SHARKER M R, CHO Y, et al.Effects of antifreeze protein Ⅲ on sperm cryopreservation of pacific abalone, Haliotis discus hannai[J].International Journal of Molecular Sciences, 2021, 22(8):3917. [53] ZILLI L, BEIRAO J, SCHIAVONE R, et al.Comparative proteome analysis of cryopreserved flagella and head plasma membrane proteins from sea bream spermatozoa:Effect of antifreeze proteins[J].Public Library of Science One, 2014, 9(6):e99992. [54] WANG S, DUAN Y, YAN Y, et al.Improvement of sperm cryo-survival of cynomolgus macaque (Macaca fascicularis) by commercial egg-yolk-free freezing medium with type Ⅲ antifreeze protein[J].Animal Reproduction Science, 2019, 210:106177. [55] QADEER S, KHAN M A, ANSARI M S, et al.Efficiency of antifreeze glycoproteins for cryopreservation of Nili-Ravi (Bubalus bubalis) buffalo bull sperm[J].Animal Reproduction Science, 2015, 157:56-62. [56] KARANOVA M V, PRONINA N D, TSVETKOVA L I.The effect of antifreeze glycoproteins on survival and quality of fish spermatozoa under the conditions of long-term storage at +4 degree C[J].Izvestiia Akademii Nauk.Seriia Biologicheskaia, 2002, l:88-92. [57] WEN Y, ZHAO S, CHAO L, et al.The protective role of antifreeze protein 3 on the structure and function of mature mouse oocytes in vitrification[J].Cryobiology, 2014, 69(3):394-401. [58] MUYASSAR A, JAELEN N M, JEREMY G, et al.Effects of antioxidants and antifreeze proteins on cryopreservation of blue catfish (Ictalurus furcatus) spermatogonia[J].Aquaculture, 2021, 531:735966. [59] YOUM H W, KIM M K, KONG H S, et al.Effects of supplementation of antifreeze proteins on follicular integrity of vitrified-warmed mouse ovary:Comparison of two types of antifreeze proteins and their combination[J].Reproductive BioMedicine Online, 2017, 35(S1):e3. [60] DOWGLISH F C, IANA S C, MIRELLY M A S S, et al.The use of antifreeze protein type Ⅲ for vitrification of in vitro matured bovine oocytes[J].Cryobiology, 2016, 73(3):324-328. [61] ARAV A, RUBINSKY B, FLETCHER G, et al.Cryogenic protection of oocytes with antifreeze proteins[J].Molecular Reproduction and Development, 1993, 36(4):488-493. [62] LEE D W, YU C Y, LEE K H.Competitive adsorption-driven separation of water/methanol mixtures using hydrogen as a third competitor[J].Journal of Colloid and Interface Science, 2009, 340(1):62-66. [63] CHAO H, DAVIES P L, CARPENTER J F.Effects of antifreeze proteins on red blood cell survival during cryopreservation[J].Journal of Experimental Biology, 1996, 199(Pt 9):2071. [64] LEE H H, LEE H J, KIM H J, et al.Effects of antifreeze proteins on the vitrification of mouse oocytes:Comparison of three different antifreeze proteins[J].Human Reproduction, 2015, 30(9):2110-2119. [65] JO J W, JEE B C, LEE J R, et al.Effect of antifreeze protein supplementation in vitrification medium on mouse oocyte developmental competence[J].Fertility and Sterility, 2011, 96(5):1239-1245. [66] KONG H S, KIM E J, YOUM H W, et al.Improvement in ovarian tissue quality with supplementation of antifreeze protein during warming of vitrified mouse ovarian tissue[J].Yonsei Medical Journal, 2018, 59(2):331. [67] ROBLES V, VALCARCE D G, RIESCO M F.The use of antifreeze proteins in the cryopreservation of gametes and embryos[J].Biomolecules, 2019, 9(5):181. [68] KIM H J, LEE J H, HUR Y B, et al.Marine antifreeze proteins:Structure, function, and application to cryopreservation as a potential cryoprotectant[J].Marine Drugs, 2017, 15(2):27. [69] LIANG S, YUAN B, JIN Y X, et al.Effects of antifreeze glycoprotein 8(AFGP8) supplementation during vitrification on the in vitro developmental capacity of expanded bovine blastocysts[J].Reproduction, Fertility, and Development, 2017, 29(11):2140-2148. [70] NISHIJIMA K, TANAKA M, SAKAI Y, et al.Effects of type Ⅲ antifreeze protein on sperm and embryo cryopreservation in rabbit[J].Cryobiology, 2014, 69(1):22-25. [71] NGUYEN T V, TANIHARA F, HIRATA M, et al.Effects of antifreeze protein supplementation on the development of porcine morulae stored at hypothermic temperatures[J].Cryo Letters, 2018, 39(2):131-136. [72] LAGNEAUX D, HUHTINEN M, KOSKINEN E, et al.Effect of anti-freeze protein (AFP) on the cooling and freezing of equine embryos as measured by DAPI-staining[J].Equine Veterinary Journal.Supplement, 1997, 25:85-87. [73] KARANOVA M V, MEZHEVIKINA L M, PETROPAVLOV N N.Study of cryoprotective properties of antifreeze glycoproteins from the white sea cod Gadus morhua on low temperature freezing of mouse embryos[J].Biofizika, 1995, 40(6):1341-1347. [74] SHAW J M, WARD C, TROUNSON A O.Evaluation of propanediol, ethylene glycol, sucrose and antifreeze proteins on the survival of slow-cooled mouse pronuclear and 4-cell embryos[J].Human Reproduction, 1995, 10(2):396-402. [75] MARTÍNEZ-PÁRAMO S, BARBOSA V, PÉREZ-CREZALES S, et al. Cryoprotective effects of antifreeze proteins delivered into zebrafish embryos[J]. Cryobiology, 2009, 58(2):128-133. [76] ROBLES V, CABRITA E, ANEL L, et al.Microinjection of the antifreeze protein type Ⅲ (AFPⅢ) in turbot (Scophthalmus maximus) embryos:Toxicity and protein distribution[J].Aquaculture, 2006, 261(4):1299-1306. [77] BAGUISI A, ARAV A, CROSBY T F, et al.Hypothermic storage of sheep embryos with antifreeze proteins:Development in vitro and in vivo[J].Theriogenology, 1997, 48(6):1017-1024. |
[1] | 黎朵, 袁鑫鑫, 沈哲弘, 阮飞, 赵璐璐, 王川坤, 曾亚琦, 姚新奎, 孟军. 补饲脯氨酸对断奶马驹生长性能、血清抗氧化和免疫指标及细胞因子含量的影响[J]. 中国畜牧兽医, 2025, 52(7): 3084-3092. |
[2] | 王茹, 王家豪, 欧靖渝, 汤文慧, 程箫, 王强军, 陈家宏, 张子军, 任春环. 抗氧化剂对反刍动物精液冷冻效果的影响[J]. 中国畜牧兽医, 2025, 52(7): 3242-3255. |
[3] | 聂晶坤, 张雅轩, 杨希妍, 王素青, 朱晓萍, 赵云翔. 杜洛克公猪精液性状的遗传参数估计[J]. 中国畜牧兽医, 2025, 52(7): 3256-3263. |
[4] | 阮诗慧, 刘春艳, 韦洋洋, 何逸懿, 吴绮雯, 熊云霞, 杨雪芬, 王丽, 易宏波. 猪δ冠状病毒对断奶仔猪肠道细胞外基质及其动态变化的影响[J]. 中国畜牧兽医, 2025, 52(7): 3297-3307. |
[5] | 张朝晖, 孙志刚, 穆祥, 冯波, 梁宏伟, 刘晓晔, 张倩. 双黄连调控跨内皮淋巴细胞抗禽流感病毒的研究[J]. 中国畜牧兽医, 2025, 52(7): 3440-3448. |
[6] | 楚洪恩, 刘源, 冯雪, 白雪, 杨梦丽, 李娟, 贺丽霞, 刘爽, 冯兰, 马云. 牛TGFB1基因克隆、生物信息学及组织表达分析[J]. 中国畜牧兽医, 2025, 52(6): 2506-2518. |
[7] | 王仲发, 刘晏辰, 闫炎, 李旻娟, 何玉楠, 关伟军, 刘文忠. 西门塔尔牛胰腺间充质干细胞分离培养及生物学特性研究[J]. 中国畜牧兽医, 2025, 52(6): 2519-2530. |
[8] | 张志浩, 鲁立刚, 张子敬, 王香南, 闵佳, 韩艺伟, 彭晟坤, 栾曼茹, 刘奥兵, 施巧婷, 王二耀. 夏南牛子宫外泌体miRNA在牛胚胎发育和着床中的作用研究[J]. 中国畜牧兽医, 2025, 52(6): 2691-2704. |
[9] | 陈丹丹, 齐雅天, 李俊杰. 卵母细胞玻璃化冷冻保存中凋亡的机制及缓解策略[J]. 中国畜牧兽医, 2025, 52(6): 2729-2735. |
[10] | 朱龙龙, 蔡龙, 刘泽青, 宋妍辰, 吴秋珏, 王晶. 异丹叶大黄素缓解IPEC-J2细胞氧化损伤的效果研究[J]. 中国畜牧兽医, 2025, 52(6): 2865-2873. |
[11] | 王楠, 杜伟伟, 王婉洁, 王悦, 袁茂莎, 聂雨欣, 孙亚茹, 刘志国, 吴添文, 牟玉莲. 基于CRISPR/Cas9基因编辑系统建立WIP1基因g.37536832 C>A位点突变的ST细胞系[J]. 中国畜牧兽医, 2025, 52(5): 1966-1976. |
[12] | 李健, 魏亚楠, 李法磊, 张慧琳, 李东伟, 刘勇, 徐高骁. lncRNA对骨骼肌卫星细胞发育的调控研究进展[J]. 中国畜牧兽医, 2025, 52(5): 2187-2197. |
[13] | 贾雨轩, 李尧江, 曾广湖, 沈祥玉, 龚婷. 从江香猪睾丸生精细胞的分离培养与鉴定[J]. 中国畜牧兽医, 2025, 52(5): 2198-2207. |
[14] | 高子浩, 李嘉, 张琳惠, 张慈, 刘炳男, 李俊杰, 夏威. 线粒体在家畜卵母细胞成熟过程中的调控机制研究进展[J]. 中国畜牧兽医, 2025, 52(5): 2232-2242. |
[15] | 黄小久, 雷磊, 彭小烨, 王开心, 陈英仪, 王济贤, 王玉格, 段德勇, 杨毅, 王爱兵. 稳定过表达NM-ⅡA Tail的IPEC-J2细胞系构建及其对PEDV感染的影响研究[J]. 中国畜牧兽医, 2025, 52(5): 2243-2252. |
阅读次数 | ||||||
全文 |
|
|||||
摘要 |
|
|||||