The Quality of Fresh and Frozen Semen and its Correlation with Molecular Weight of Seminal Plasma Protein in Bali Cattle
Abstract
This study evaluated the quality of fresh and frozen semen of Bali cattle and its correlation with the molecular weight (MW) of seminal plasma protein. This study collected semen from 10 bulls aged 5–10 years using an artificial vagina and evaluated the samples macroscopically and microscopically. Two batches of frozen semen obtained in 2020 and 2021 were also analyzed. The frozen semen samples were thawed at 37 °C for 30 seconds. The sperm motility, viability, intact plasma membrane (IPM), and sperm abnormalities were investigated. The concentration of the seminal plasma proteins was determined using the Bradford method, and the proteins were characterized using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (1D-SDS-PAGE). Additionally, the gels were stained with Coomassie brilliant blue, and the MWs of the proteins were determined using MW markers. The sperm motility, viability, and abnormalities of fresh semen varied significantly among the bulls (p<0.05); however, sperm IPMs among the bulls were similar (p>0.05). No differences in sperm motility after freezing were found among the bulls. However, the sperm viability, abnormality, and IPM varied among the bulls. Meanwhile, the seminal plasma proteins contained bands with different MWs. No difference in the expression of protein bands between bulls. Linearity analysis showed that sperm motility (r= 0.281), viability (r= 0.189), abnormalities (r= 0.141), and IPM (r= 0.173) were positively correlated with the protein bands at each MW (p<0.05). The results conclude there was a positive correlation between the MW of the protein marker and the same protein expression levels in Bali bulls. Therefore, the band intensity of Bali cattle seminal plasma proteins can be used as a biomarker for selecting superior Bali bulls.
References
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Baharun, A., R. I. Arifiantini, N. W. K. Karja, & S. Said. 2021. Seminal plasma protein profile based on molecular weight and the correlation with semen quality of Simmental bull. J. Indones. Trop. Anim. Agric. 46:20-28. https://doi.org/10.14710/jitaa.46.1.20-28
Beran, J., O. Simonik, & L. Standik. 2013. Effect of bull, diluter, and LDL-Cholesterol concentration on spermatozoa resistance against cold shock. Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 173:1575-1581. https://doi.org/10.11118/actaun201361061575
Bradford, M. M. 1976. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. https://doi.org/10.1016/0003-2697(76)90527-3
BSN (Badan Standardisasi Nasional). 2017. SNI Semen Beku- Bagian 1: Sapi. BSN, Jakarta.
Chacur, M. G. M. 2012. Seminal plasma proteins as potential markers of relative fertility in Zebu bulls (Bos taurus-indicus). Electrophoresis 173-193.
De Lazari, F. L., E. R. Sontag, A. Scheinder, A. A. A. Moura, F. R. Vascocoles, S. S. Nagano, R. C. Mattos, M. I. N. Jobim, & I. C. B. Filho. 2018. Seminal plasma proteins and their relationship with sperm motility and morphology in boars. Andrologia 51:e13222. https://doi.org/10.1111/and.13222
Diskin, M. G., P. Lonergan, D. A. Kenny, & S. Fair. 2018. International bull fertility conference-Theory to practice, Westport, Ireland. Animal 12:s1-s3. https://doi.org/10.1017/S1751731118001155
Druart, X. & S. de Graaf. 2019. Seminal plasma proteomes and sperm fertility. Anim. Reprod. Sci. 194:33-40. https://doi.org/10.1016/j.anireprosci.2018.04.061
Druart, X., J. P. Rickard, S. Mactier, P. L. Kohnke, C. M. Kershaw-Young, R. Bathgate, Z. Gibb, B. Crossett, G. Tsikis, V. Labas, G. Harichaux, C. G. Grupen, & S. P. de Graaf. 2013. Proteomic characterization and cross-species comparison of seminal mammalian plasma. Proteomics 91:13-22. https://doi.org/10.1016/j.jprot.2013.05.029
Fonseca, J. F., C. A. A. Torres, V. V. Maffili, A. M. Borges, A. D. F. Santos, M. T. Rodrigues, & R. F. M. Oliveira. 2005. The hypoosmotic swelling test in fresh goat spermatozoa. Anim. Reprod. 2:139-144.
Fraser, L., Z. J. Strze, & W. Kordan. 2014. Post-thaw sperm characteristics following long-term storage of boar semen in liquid nitrogen. Anim. Reprod. Sci. 147:119-127. https://doi.org/10.1016/j.anireprosci.2014.04.010
Frayne, J. & L. Hall. 2002. A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring protein complex, rather than a unique role in sperm-zona pellucida binding. Reproduction 124:767-774. https://doi.org/10.1530/rep.0.1240767
Fu, Q., L. Pan, D. Huang, Z. Wang, Z. Hou, & M. Zhang. 2019. Proteomic profiles of buffalo spermatozoa and seminal plasma. Theriogenology 134:74-82. https://doi.org/10.1016/j.theriogenology.2019.05.013
Govindaraju, A., A. Uzun, L. Robertson, M. O. Atli, A. Kaya, E. Topper, E. A. Crate, J. Padbury, A. Perkins, & E. Meili. 2012. Dynamics of microRNAs in bull spermatozoa. Reprod. Biol. Endocrinol. 14:10:82. https://doi.org/10.1186/1477-7827-10-82
Hillman, P., D. Lckowicz, R. Vizel, & H. Breitbart. 2013. Dissociation between AKAP3 and PKARII promotes AKAP3 degradation in sperm capacitation. PLoS ONE 8:e68873. https://doi.org/10.1371/journal.pone.0068873
Indriastuti, R., M. F. Ulum, R. I. Arifiantini, & B. Purwantara. 2020. Individual variation in fresh and frozen semen of Bali bulls (Bos sondaicus). Vet. World. 13:840 846. https://doi.org/10.14202/vetworld.2020.840-846
Ismirandy, A., H. Sonjaya, & H. Hasbi. 2021. The outcome of in vitro transfer on Bali cattle by utilizing fresh dan frozen embryos. Int. J. Sci. Basic Appl. Res. 50:200-206.
Karunakaran, M., V. C. Gajare, A. Mandal, M. Mondal, S. K. Das, M. K. Ghosh, S. Rai, & R. Bahera. 2019. Electrophoretic of seminal proteins and their correlation with in vitro sperm characters in Black Bengal buck semen. Vet. World. 12:621-628. https://doi.org/10.14202/vetworld.2019.621-628
Lisson, S., N. MacLeod, C. McDonald, J. Corfield, B. Pengelly, L. Wirajaswadi, R. Rahman, S. Bahar, R. Padjung, N. Razak, & K. Puspadi. 2010. A participatory farming systems approach to improving Bali cattle production in the smallholder crop-livestock systems of Eastern Indonesia. Agric. Syst. 103:486-497. https://doi.org/10.1016/j.agsy.2010.05.002
Lu, C. H., R. K. K. Lee, Y. M. Hwu, S. L. Chu, Y. J. Chen, W. C. Chang, S. P. Lin, & S. H. Li. 2011. SERPINE2, a serine protease inhibitor extensively expressed in adult male mouse reproductive tissues, may serve as a murine sperm decapacitation factor. Biol. Reprod. 84:514-525. https://doi.org/10.1095/biolreprod.110.085100
Moura, A. A., C. E. Souza, B. A. Stanley, D. A. Chapman, & G. J. Killian. 2010. Proteomics of cauda epididymal fluid from mature Holstein bulls. J. Proteomics. 73:2006-2020. https://doi.org/10.1016/j.jprot.2010.06.005
Ntemka, A., G. Tsousis, C. Brozos, E. Kiossis, C. M. Boscos, & I. A. Tsakmakidis. 2016. Breed differences of bull frozen-thawed semen. Reprod. Domest. Anim. 51:945-952. https://doi.org/10.1111/rda.12769
Park, Y. J., W. S. Kwon, S. A. Oh, & M. G. Pang. 2012. Fertility-related proteomic profiling bull spermatozoa separated by Percoll. J. Proteome. Res. 11:4162−4168. https://doi.org/10.1021/pr300248s
Purdy, P. 2006. A review on goat sperm cryopreservation. Small Rumin. Res. 63:215-225. https://doi.org/10.1016/j.smallrumres.2005.02.015
Purwantara, B., R. R. Noor, G. Andersson, & H. Rodriguez-Martinez. 2012. Banteng and Bali cattle in Indonesia: Status and forecasts. Reprod. Domest. Anim. 47:2–6. https://doi.org/10.1111/j.1439-0531.2011.01956.x
Recuero, S., B. Fernandez-Fuertes, S. Bonet, I. Barranco, & M. Yeste. 2019. Potential of seminal plasma to improve the fertility of frozen-thawed boar spermatozoa. Theriogenology 137:36–42. https://doi.org/10.1016/j.theriogenology.2019.05.035
Rego, J. P. A., J. M. Crisp, A. A. Moura, A. S. Nouwens, Y. Li, B. Venus, N. J. Corbet, D. H. Corbet, B. M. Burns, G. B. Boe-Hansen, & M. R. McGowan. 2014. Seminal plasma proteome of electroejaculation Bos indicus bulls. Anim. Reprod. Sci. 148:1–17. https://doi.org/10.1016/j.anireprosci.2014.04.016
Rodriguez-Villamil, P., V. Hoyos-Marulanda, J. A. M. Martins, A. N. Oliveira, L. H. Aguiar, F. B. Moreno, A. L. M. C. S. Velho, A. C. Monteiro-Moreira, R. A. Moreira, I. M. Vasconcelos, M. Bertolini, & A. A. Moura. 2016. Purification of binder of sperm protein 1 (BSP1) and its effects on bovine in vitro embryo development after fertilization with ejaculated and epididymal sperm. Theriogenology 85:540-554. https://doi.org/10.1016/j.theriogenology.2015.09.044
Rosyada, Z. N. A., M. F. Ulum, L. I. T. A. Tumbelaka, & B. Purwantara. 2020. Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia. Vet. World. 13:947-955. https://doi.org/10.14202/vetworld.2020.947-955
Santoso, S., R. I. Herdis, Arifiantini, A. Gunawan, & C. Sumantri. 2021. Characteristics and potential production of frozen semen of Pasundan bull. Trop. Anim. Sci. J. 44:24-31. https://doi.org/10.5398/tasj.2021.44.1.24
Samanta, L., R. Parida, T. R. Dias, & A. Agarwal. 2018. The enigmatic seminal plasma: a proteomics insight from ejaculation to fertilization. Reprod. Biol. Endocrinol. 16:1-11. https://doi.org/10.1186/s12958-018-0358-6
Sarsaifi, K., A. W. Haron, J. Vijayan, R. Yusoff, H. Hani, M. A. Omar, L. W. Hong, N. Yimer, T. Y. Ju, & A. M. Othman. 2015. Two-dimensional polyacrylamide gel electrophoresis of Bali bull (Bos javanicus) seminal plasma proteins and their relationship with semen quality. Theriogenology 84:956-968. https://doi.org/10.1016/j.theriogenology.2015.05.035
Schneider, C. A., W. S. Rasband, & K. W. Eliceiri. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 9:671-675. https://doi.org/10.1038/nmeth.2089
Sieme, H., H. Oldenhof, & W. F. Wolkers. 2015. Sperm membrane behavior during cooling and cryopreservation. Reprod. Domest. Anim. 50:20-26. https://doi.org/10.1111/rda.12594
Subagyo, W. C., N. K. Suwiti, & I. N. Suarsana. 2015. The protein characteristics of Bali and wagyu beef boiled. Buletin Veteriner Udayana 7:17-25.
Sunter, J. D., V. Varga, S. Dean, & K. Gull. 2015. A dynamic coordination of flagellum and cytoplasmic cytoskeleton assembly specifies cell morphogenesis in trypanosomes. J. Cell. Sci. 128:1580-1594. https://doi.org/10.1242/jcs.166447
Sutarno, D. & A. D. Setyawan. 2016. Review: The diversity of local cattle in Indonesia and the efforts to develop superior indigenous cattle breeds. Biodiv. J. Bio. Div. 17:275-295. https://doi.org/10.13057/biodiv/d170139
Tahuk, P. K., S. P. S. Budhi, Panjono, & E. Baliarti. 2018. Carcass and meat characteristics of male Bali cattle in Indonesian smallholder farms fed ration with different protein levels. Trop. Anim. Sci. J. 41:215-223. https://doi.org/10.5398/tasj.2018.41.3.215
Thundathil, J. C., A. L. Dance, & J. P. Kastelic. 2016. Fertility management of bulls to improve beef cattle productivity. Theriogenology 86:397-405. https://doi.org/10.1016/j.theriogenology.2016.04.054
Wahyu, T. U., I. N. Suarsana, & I. G. A. A. Suartini. 2017. Characteristics of Bali cattle plasma proteins. Jurnal Veteriner 18:232-238. https://doi.org/10.19087/jveteriner.2017.18.2.232
Wasilewska, K. & L. Fraser. 2017. Boar variability in sperm cryo-tolerance after cooling of semen in different long-term extenders at various temperatures. Anim. Reprod. Sci. 185:161-173. https://doi.org/10.1016/j.anireprosci.2017.08.016
Yeste, M. 2016. Sperm cryopreservation update: Cryodamage, markers, and factors affecting the sperm freezability in pigs. Theriogenology 85:47–64. https://doi.org/10.1016/j.theriogenology.2015.09.047
Yoon, S. J., M. S. Rahman, W. S. Kwon, D. Y. Ryu, Y. J. Park, & M. G. Pang. 2016. Proteomic identification of cryostress in epididymal spermatozoa. J. Anim. Sci. Biotechnol. 7:67. https://doi.org/10.1186/s40104-016-0128-2
Zhang, X. G., S. Hu, C. Han, Q. C. Zhu, G. J. Yan, & J. H. Hu. 2015. Association of heat shock protein 90 with motility of post-thawed sperm in bulls. Cryobiology 70:164-169. https://doi.org/10.1016/j.cryobiol.2014.12.010
Zubair, M., M. Ahmad, & H. Jamil. 2014. Review on the screening of semen by hypo-osmotic swelling test. Andrologia 47:744-50. https://doi.org/10.1111/and.12335
Baharun, A., R. I. Arifiantini, N. W. K. Karja, & S. Said. 2021. Seminal plasma protein profile based on molecular weight and the correlation with semen quality of Simmental bull. J. Indones. Trop. Anim. Agric. 46:20-28. https://doi.org/10.14710/jitaa.46.1.20-28
Beran, J., O. Simonik, & L. Standik. 2013. Effect of bull, diluter, and LDL-Cholesterol concentration on spermatozoa resistance against cold shock. Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 173:1575-1581. https://doi.org/10.11118/actaun201361061575
Bradford, M. M. 1976. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. https://doi.org/10.1016/0003-2697(76)90527-3
BSN (Badan Standardisasi Nasional). 2017. SNI Semen Beku- Bagian 1: Sapi. BSN, Jakarta.
Chacur, M. G. M. 2012. Seminal plasma proteins as potential markers of relative fertility in Zebu bulls (Bos taurus-indicus). Electrophoresis 173-193.
De Lazari, F. L., E. R. Sontag, A. Scheinder, A. A. A. Moura, F. R. Vascocoles, S. S. Nagano, R. C. Mattos, M. I. N. Jobim, & I. C. B. Filho. 2018. Seminal plasma proteins and their relationship with sperm motility and morphology in boars. Andrologia 51:e13222. https://doi.org/10.1111/and.13222
Diskin, M. G., P. Lonergan, D. A. Kenny, & S. Fair. 2018. International bull fertility conference-Theory to practice, Westport, Ireland. Animal 12:s1-s3. https://doi.org/10.1017/S1751731118001155
Druart, X. & S. de Graaf. 2019. Seminal plasma proteomes and sperm fertility. Anim. Reprod. Sci. 194:33-40. https://doi.org/10.1016/j.anireprosci.2018.04.061
Druart, X., J. P. Rickard, S. Mactier, P. L. Kohnke, C. M. Kershaw-Young, R. Bathgate, Z. Gibb, B. Crossett, G. Tsikis, V. Labas, G. Harichaux, C. G. Grupen, & S. P. de Graaf. 2013. Proteomic characterization and cross-species comparison of seminal mammalian plasma. Proteomics 91:13-22. https://doi.org/10.1016/j.jprot.2013.05.029
Fonseca, J. F., C. A. A. Torres, V. V. Maffili, A. M. Borges, A. D. F. Santos, M. T. Rodrigues, & R. F. M. Oliveira. 2005. The hypoosmotic swelling test in fresh goat spermatozoa. Anim. Reprod. 2:139-144.
Fraser, L., Z. J. Strze, & W. Kordan. 2014. Post-thaw sperm characteristics following long-term storage of boar semen in liquid nitrogen. Anim. Reprod. Sci. 147:119-127. https://doi.org/10.1016/j.anireprosci.2014.04.010
Frayne, J. & L. Hall. 2002. A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring protein complex, rather than a unique role in sperm-zona pellucida binding. Reproduction 124:767-774. https://doi.org/10.1530/rep.0.1240767
Fu, Q., L. Pan, D. Huang, Z. Wang, Z. Hou, & M. Zhang. 2019. Proteomic profiles of buffalo spermatozoa and seminal plasma. Theriogenology 134:74-82. https://doi.org/10.1016/j.theriogenology.2019.05.013
Govindaraju, A., A. Uzun, L. Robertson, M. O. Atli, A. Kaya, E. Topper, E. A. Crate, J. Padbury, A. Perkins, & E. Meili. 2012. Dynamics of microRNAs in bull spermatozoa. Reprod. Biol. Endocrinol. 14:10:82. https://doi.org/10.1186/1477-7827-10-82
Hillman, P., D. Lckowicz, R. Vizel, & H. Breitbart. 2013. Dissociation between AKAP3 and PKARII promotes AKAP3 degradation in sperm capacitation. PLoS ONE 8:e68873. https://doi.org/10.1371/journal.pone.0068873
Indriastuti, R., M. F. Ulum, R. I. Arifiantini, & B. Purwantara. 2020. Individual variation in fresh and frozen semen of Bali bulls (Bos sondaicus). Vet. World. 13:840 846. https://doi.org/10.14202/vetworld.2020.840-846
Ismirandy, A., H. Sonjaya, & H. Hasbi. 2021. The outcome of in vitro transfer on Bali cattle by utilizing fresh dan frozen embryos. Int. J. Sci. Basic Appl. Res. 50:200-206.
Karunakaran, M., V. C. Gajare, A. Mandal, M. Mondal, S. K. Das, M. K. Ghosh, S. Rai, & R. Bahera. 2019. Electrophoretic of seminal proteins and their correlation with in vitro sperm characters in Black Bengal buck semen. Vet. World. 12:621-628. https://doi.org/10.14202/vetworld.2019.621-628
Lisson, S., N. MacLeod, C. McDonald, J. Corfield, B. Pengelly, L. Wirajaswadi, R. Rahman, S. Bahar, R. Padjung, N. Razak, & K. Puspadi. 2010. A participatory farming systems approach to improving Bali cattle production in the smallholder crop-livestock systems of Eastern Indonesia. Agric. Syst. 103:486-497. https://doi.org/10.1016/j.agsy.2010.05.002
Lu, C. H., R. K. K. Lee, Y. M. Hwu, S. L. Chu, Y. J. Chen, W. C. Chang, S. P. Lin, & S. H. Li. 2011. SERPINE2, a serine protease inhibitor extensively expressed in adult male mouse reproductive tissues, may serve as a murine sperm decapacitation factor. Biol. Reprod. 84:514-525. https://doi.org/10.1095/biolreprod.110.085100
Moura, A. A., C. E. Souza, B. A. Stanley, D. A. Chapman, & G. J. Killian. 2010. Proteomics of cauda epididymal fluid from mature Holstein bulls. J. Proteomics. 73:2006-2020. https://doi.org/10.1016/j.jprot.2010.06.005
Ntemka, A., G. Tsousis, C. Brozos, E. Kiossis, C. M. Boscos, & I. A. Tsakmakidis. 2016. Breed differences of bull frozen-thawed semen. Reprod. Domest. Anim. 51:945-952. https://doi.org/10.1111/rda.12769
Park, Y. J., W. S. Kwon, S. A. Oh, & M. G. Pang. 2012. Fertility-related proteomic profiling bull spermatozoa separated by Percoll. J. Proteome. Res. 11:4162−4168. https://doi.org/10.1021/pr300248s
Purdy, P. 2006. A review on goat sperm cryopreservation. Small Rumin. Res. 63:215-225. https://doi.org/10.1016/j.smallrumres.2005.02.015
Purwantara, B., R. R. Noor, G. Andersson, & H. Rodriguez-Martinez. 2012. Banteng and Bali cattle in Indonesia: Status and forecasts. Reprod. Domest. Anim. 47:2–6. https://doi.org/10.1111/j.1439-0531.2011.01956.x
Recuero, S., B. Fernandez-Fuertes, S. Bonet, I. Barranco, & M. Yeste. 2019. Potential of seminal plasma to improve the fertility of frozen-thawed boar spermatozoa. Theriogenology 137:36–42. https://doi.org/10.1016/j.theriogenology.2019.05.035
Rego, J. P. A., J. M. Crisp, A. A. Moura, A. S. Nouwens, Y. Li, B. Venus, N. J. Corbet, D. H. Corbet, B. M. Burns, G. B. Boe-Hansen, & M. R. McGowan. 2014. Seminal plasma proteome of electroejaculation Bos indicus bulls. Anim. Reprod. Sci. 148:1–17. https://doi.org/10.1016/j.anireprosci.2014.04.016
Rodriguez-Villamil, P., V. Hoyos-Marulanda, J. A. M. Martins, A. N. Oliveira, L. H. Aguiar, F. B. Moreno, A. L. M. C. S. Velho, A. C. Monteiro-Moreira, R. A. Moreira, I. M. Vasconcelos, M. Bertolini, & A. A. Moura. 2016. Purification of binder of sperm protein 1 (BSP1) and its effects on bovine in vitro embryo development after fertilization with ejaculated and epididymal sperm. Theriogenology 85:540-554. https://doi.org/10.1016/j.theriogenology.2015.09.044
Rosyada, Z. N. A., M. F. Ulum, L. I. T. A. Tumbelaka, & B. Purwantara. 2020. Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia. Vet. World. 13:947-955. https://doi.org/10.14202/vetworld.2020.947-955
Santoso, S., R. I. Herdis, Arifiantini, A. Gunawan, & C. Sumantri. 2021. Characteristics and potential production of frozen semen of Pasundan bull. Trop. Anim. Sci. J. 44:24-31. https://doi.org/10.5398/tasj.2021.44.1.24
Samanta, L., R. Parida, T. R. Dias, & A. Agarwal. 2018. The enigmatic seminal plasma: a proteomics insight from ejaculation to fertilization. Reprod. Biol. Endocrinol. 16:1-11. https://doi.org/10.1186/s12958-018-0358-6
Sarsaifi, K., A. W. Haron, J. Vijayan, R. Yusoff, H. Hani, M. A. Omar, L. W. Hong, N. Yimer, T. Y. Ju, & A. M. Othman. 2015. Two-dimensional polyacrylamide gel electrophoresis of Bali bull (Bos javanicus) seminal plasma proteins and their relationship with semen quality. Theriogenology 84:956-968. https://doi.org/10.1016/j.theriogenology.2015.05.035
Schneider, C. A., W. S. Rasband, & K. W. Eliceiri. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 9:671-675. https://doi.org/10.1038/nmeth.2089
Sieme, H., H. Oldenhof, & W. F. Wolkers. 2015. Sperm membrane behavior during cooling and cryopreservation. Reprod. Domest. Anim. 50:20-26. https://doi.org/10.1111/rda.12594
Subagyo, W. C., N. K. Suwiti, & I. N. Suarsana. 2015. The protein characteristics of Bali and wagyu beef boiled. Buletin Veteriner Udayana 7:17-25.
Sunter, J. D., V. Varga, S. Dean, & K. Gull. 2015. A dynamic coordination of flagellum and cytoplasmic cytoskeleton assembly specifies cell morphogenesis in trypanosomes. J. Cell. Sci. 128:1580-1594. https://doi.org/10.1242/jcs.166447
Sutarno, D. & A. D. Setyawan. 2016. Review: The diversity of local cattle in Indonesia and the efforts to develop superior indigenous cattle breeds. Biodiv. J. Bio. Div. 17:275-295. https://doi.org/10.13057/biodiv/d170139
Tahuk, P. K., S. P. S. Budhi, Panjono, & E. Baliarti. 2018. Carcass and meat characteristics of male Bali cattle in Indonesian smallholder farms fed ration with different protein levels. Trop. Anim. Sci. J. 41:215-223. https://doi.org/10.5398/tasj.2018.41.3.215
Thundathil, J. C., A. L. Dance, & J. P. Kastelic. 2016. Fertility management of bulls to improve beef cattle productivity. Theriogenology 86:397-405. https://doi.org/10.1016/j.theriogenology.2016.04.054
Wahyu, T. U., I. N. Suarsana, & I. G. A. A. Suartini. 2017. Characteristics of Bali cattle plasma proteins. Jurnal Veteriner 18:232-238. https://doi.org/10.19087/jveteriner.2017.18.2.232
Wasilewska, K. & L. Fraser. 2017. Boar variability in sperm cryo-tolerance after cooling of semen in different long-term extenders at various temperatures. Anim. Reprod. Sci. 185:161-173. https://doi.org/10.1016/j.anireprosci.2017.08.016
Yeste, M. 2016. Sperm cryopreservation update: Cryodamage, markers, and factors affecting the sperm freezability in pigs. Theriogenology 85:47–64. https://doi.org/10.1016/j.theriogenology.2015.09.047
Yoon, S. J., M. S. Rahman, W. S. Kwon, D. Y. Ryu, Y. J. Park, & M. G. Pang. 2016. Proteomic identification of cryostress in epididymal spermatozoa. J. Anim. Sci. Biotechnol. 7:67. https://doi.org/10.1186/s40104-016-0128-2
Zhang, X. G., S. Hu, C. Han, Q. C. Zhu, G. J. Yan, & J. H. Hu. 2015. Association of heat shock protein 90 with motility of post-thawed sperm in bulls. Cryobiology 70:164-169. https://doi.org/10.1016/j.cryobiol.2014.12.010
Zubair, M., M. Ahmad, & H. Jamil. 2014. Review on the screening of semen by hypo-osmotic swelling test. Andrologia 47:744-50. https://doi.org/10.1111/and.12335
Authors
IskandarH., SonjayaH., ArifiantiniR. I., & HasbiH. (2022). The Quality of Fresh and Frozen Semen and its Correlation with Molecular Weight of Seminal Plasma Protein in Bali Cattle. Tropical Animal Science Journal, 45(4), 405-412. https://doi.org/10.5398/tasj.2022.45.4.405
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