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GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM

Year 2009, Volume: 35 Issue: 2, 1 - 12, 20.11.2012

Abstract

ABSTRACT

Bio-active compounds from marine flora and fauna contain various types of pharmacologically active novel biomolecules enriched with different types of lectins. Lectins, with high saccharide binding specificities have been considered important probe to monitor the changes in plasmamembrance during physiological maturation of spermatozoa. Cytosol fraction, isolated from the spermatheca and / or ovotestis gland of a marine mollusc Telescopium telescopium, specific for sialic acid, has been found responsible for "Head to Head" sperm agglutination, and the agglutinability varies in number (p<0.01) among the epididymal regions. Number of hypo-osmotic swelling-positive spermatozoa also exhibited region wise variation (p<0.01) where both the characters remained maximum in caudal region. The differences in the number of agglutinating spermatozoa and their pattern reflects modification of sperm surface carbohydrate moieties linked either with lipid or protein that occur during epididymal transit and heterogenic nature was due to regional variation in the carbohydrate domain of sperm plasmamembrane. Differences (P<0.01) in the number of hypo-osmotic swelling-positive spermatozoa between the epididymal regions indicated sperm plasmamembrane in the caput are less permeable and less functional than spermatozoa from corpus and caudal segment. These indicated maturation along with alteration of sperm plasmamembrane occurs gradually during epididymal passage. Present approach with this bio-active compound obtained from marine snail could be used as a biomarker to study the sperm maturation process, and heterogeneity and status of the plasmamembrane which might help to improve the diagnosis of reproductive problems in relation to distribution of lectin receptors on sperm cells of any species to predict status of the male gametes before use in artificial reproductive technologies.

Key Words: Sperm plasmamembrane, Telescopium telescopium, agglutination, lectin.

 

EPİDİDİMAL OLGUNLAŞMA SIRASINDA KEÇİ SPERMA YÜZEYİNDE MEYDANA GELEN DEĞİŞİMLER: DENİZ BİOAKTİF BİLEŞİMİ OLAN TELESKOPİUM TELESKOPİUM 'UN DEĞERLENDİRİLMESİ

ÖZET

Deniz florası ve faunasının bio-aktif yapıları farmakolojik olarak aktif ve değişik bimolekülleri içerirler ve bu moleküller çeşitli lektinlerle zenginleştirilmiştir. Lektinler, yüksek oranda sakkarit bağları ile özelleşmişlerdir ve spermanın olgunlaşması sırasında plazma membranında meydana gelen fizyolojik değişimlerin izlenmesi araştırılmalarında bu lektinler önemli oranda düşünülmelidir. Deniz yumuşakçalarından olan teleskopium teleskopiumun ovotestis bezinden ve/veya spermatekadan izole edilen sitoplazma fraksiyonu sialik asit açısından spesifiktir ve bu spermanm baş başa olan aglütinasyonundan sorumlu bulunmuştur ve aynı zamanda epididimal bölgeler arasında aglutine olabilirliği P<0.01 dir. Aynı zamanda, çok sayıda hipoosmotik şişme-positive spermatozoa mevcut bölgede geniş oranda bulunmuş P<0.01 ve her iki özellikte kaudal bölgede maksimum oranda saptanmıştır. Aglutine olan spermatozoonların sayısında ve şekillerindeki (aglutine olma şekli) degişiklikler spermatozoitlerin yüzeyindeki yağ ve proteinlere bağlı karbonhidratlardaki farkhhklari gostermekte ve bu farklılıkların epididimal geçiş sırasında ortaya çıktığını ve bu değişikliklerin sperma plazma membranının ana karbonhidrat yapısını etkilediğini göstermektedir. Epididimal bölgeler arasında çok sayıdaki hipoosmotik şişme pozitif spermatozoa farkı P<0.01, kaput bölgesindeki sperma plazma membranının korpus ve kaudal bölgedeki spermadan daha az geçirgen ve daha az fonksiyonel olduğuna işaret eder. Sperma plazma membranındaki degişiklerle ilgili olan bu belirlenmiş olgunlaşma kademe kademe epididaml bölgede meydana gelir. Mevcut bilgilerle, deniz yumuşakçalarından elde edilen bu bio-aktif bileşik spermanın olgunlaşması çalışmalarında biomarker olarak kullanılabilir ve ayrıca suni üreme teknolojilerinde kullanılmadan önce sperm hücrelerinin üzerindeki lektin reseptörlerinin dağılımı ile ilişkili olan reprodüktif problemlerinin tanısını geliştirmede yardımcı olacak heterojenlikve plazma membran durumunu belirlemede kullanılabilir.

Anahtar Kelimeler: Sperm plazmamembrani, Teleskopium teleskopium, aglutinasyon, lektin

References

  • Arya, M., Vanha-Perttula, T.: Lectin binding pattern of bull testis and epididymis. J. Androl.,(1985a);6: 230-242.
  • Bedford, J . M.: Maturation, transport & fate of spermatozoa in the epididymis. Handbook of physiology, Vol. V., Section-6, (cd.) Hamilton, D.W. & Green, R. O. Am. Phy. Soc, Washington D.C., (1975); 307-317.
  • Bernal, A., Torres, J . , Reyes, A., Rosado, A.: Presence and regional distribution of sialyl transferase in the epididymis of the rat. Biol. Reprod., (1980); 23: 290-293.
  • Briz, M. D., Bond, S., Pinart, B., Egozcue, J . , Camps, R.: Comparative study of boar sperm coming from the caput, corpus and cauda regions of the epididymis. J. Androl., (1995); 16(2): 175-188.
  • Brooks, D. E.: Secretion of proteins and glycoproteins by the rat epididymis: regional differences, androgen dependence, and effects of protease inhibitors, procaine, and tunicamycin. Biol. Reprod., (1981); 25: 1091-1097.
  • Datta, U.: Bioactivc substance(s) from a marine mollusc Telcscopium telcscopium and its role on mammalian reproduction. Ph.D. Thesis. Jadavpur University, Kolkata, India. 2003.
  • Drevius, L . O.: Bull spermatozoa as osmometers. J. Reprod. Fertility., (1972); 28: 29-39.
  • Duncan, D. B.: Multiple range and multiple F test. Biometrics., (1955); 11: 1-42.
  • Frazier, W., Glaser, L . : Surface components and cell recognition. Annu. Rev. Biochem.. (1979); 48: 491-496.
  • Gabius, H-J.: Vertebrate lectins and their possible role in fertilization, development and tumor biology. ln-vitro., (1987); 1: 75-84.
  • Goldstein, I. J . , Hayes, C. E.: The lectins: carbohydrate binding proteins of plants and animals. Adr. Carhydr. Chem. Biochem., (1978); 35: l'27-340.
  • Green, D. P.: Mammalian fertilization as a biological machine: a working model for adhesion and fusion of sperm and oocyte. Human Reprod., (1993): 8: 91-96.
  • Gwatkin, R., Williams, D.: Receptor activity of the solubilized hampster and mouse zona pellucida before and after the zona reaction. J. Reprod. Fetil., (1976); 19: 55-59.
  • Hinton, B. T., Palladino, M. A.: Epididymal epithelium: its contribution to the formation of a luminal fluid microenvironment. Micros. Res. Tech., (1995); 30: 67-81.
  • Jeyendran, R. S., Vandervent, H. H., Perez-Paleac, Z. M., Crabo, B. G., Zanevld, L . J . D.: Development of an assay to assess the functional integrity of human sperm membrane and its relationship to other semen characteristics. J. Reprod. Fcrtil., (1984); 70: pp. 219ı 225.
  • Jones, R.: Membrane remodeling during sperm maturation in the epididymis. Oxford Reviews of Reproductive Biology, (1989); 1: 285-337. Gout Sperm Surface Alteration During Epididymal Maturation An Avaluation 11
  • Jones, R., Brown, C. R., Von Gios, K. I., Parker, M . G.: Hormonal regulation of protein synthesis in the rai epididymis. Characterization of androgen-dependent and testicular fluid- dependent proteins. Biochem. J., (1980); 188: 667-676.
  • Koehler, J. K.: Lectins as probes of the spermatozoan surface. Arch. Androl., (1981); 6: 197-217.
  • Kunz, A., Brown, D., Orci, L . : Appearance of helix pomatia lectin binding sites on podocytc plasma membrane during glomerular differentiation. A quantitivc analysis using the lectin-gold technique. Lab. Invest., (1984); 51 (3): 317-324.
  • Levine, N., Marsh, D. J.: Micro puncture studies of the electrochemical aspects of fluid and electrolyte transport in individual seminiferous tubules, the epididymis and the vas deferens in rats. J. Physiol., (1971); 213 (3): 557-570.
  • Lis, H., Sharon, IN.: Lectins as molecules and as tools. Ann. Rev. Biochem., (1986); 55: pp. 35-67.
  • L i u , H. W., L i n , Y. C , Chao, C. F., Chang, S. Y., Sun, G. H . : GP-83 and GP-39, two glycoprotein secreted by human epididymis are conjugated to spermatozoa during maturation. Mol Human Reprod., (2000); 6 (5): 422-428.
  • Lopez, M . L . , deSouza. W., Bustos-Obregon, E.: C>tochemical analysis o f the anionic sites on the membrane o f the stallion spermatozoa during the epididymal transit. Gamete Res., (19S9); 18: pp.319-332.
  • Lowry, O. I L , Rosebrough, N . J., Farr, A. 1., Randall, R. J.: Protein measurement with the folin-phenol reagent. J. Biochem., (1951); 193, 265.
  • Mladenovic, L, Hajducovic. L.. Genbacev, O., Cuperlovic, M . , Movsesijan, M . : Lectin binding as a biological test in vitro for the prediction of functional activity of human spermatozoa. Gamete Res., (1993); 24: 403-413.
  • Monsigny, M . , Roche, A. C Kirnda. C , Midoux, P., Obernovitch, A.: Characterization and biological implications o f membrane lectins in tumors, lyphoid and myeloid cells. Biochem., (1988); 70: 1633-1649.
  • Moore, H . D. M . : Contribution of epididymal factors to sperm maturation and storage. Andrologia., (1998); 30: 233-239.
  • M vies, D. G.: Molecular mechanisms of sperm-egg membrane binding and fusion in mammals. Dev. Biol., (1993); ¡58: 35-45.
  • Nicolson, G. L . : The interactions of lectins with animal cell surfaces. Int. Rev. Cytol., (1974); 39:90-190.
  • Pakrashi, A., Datta, U.: in-vitro sperm agglutination and spermicidal activity o f protein isolated from a marine mollusc Telescopium telescopium (Gastropod). Indian J. Marine Sci., (2001); 30: 93-97.
  • Peleg, B. A., Ian Consscu, M . : Sperm agglutination and sperm absorption due to mixoviruses. Nature., ( 1966); 211:1211-1212.
  • Sanz, I . , Calvete, J. J., Mann, K., Gabius, H. J., Topfer-petersen, E.: Isolation and biochemical characterization of heparin binding protein from boar seminal plasma a dual role for sperm adhesion in fertilization. Mol. Reprod. Dev., (1993); 34: 37-43.
  • Sarkar, M . , Mazurndar, G. C , Chatterjee, T.: Goat sperm membrane: Lectin binding sites of sperm surface and lectin affinity chromatography o f the mature sperm membrane antigens. Biochion. Biophys. Acta., ( 1991); 1070(1); 19S-204.
  • Manik Lai HEMBRAM-Uttam D ATT A-Raj u DASGUPTA
  • Schwarz, M. A., Koehler, J . K.: Alteration in lectin binding to guineapig spermatozoa accompanying in vitro capacitation and acrosomc reaction. Biol. Reproduction, (1979); 21:1295-1299.
  • Serrano, H., Díaz-Esparza, L . , Garcia-Suarez, D.: Pig sperm membrane integrity evaluated by lectin labeling. Arch. Androl., (2001); 47 (1): 59-65.
  • Signer, S. L . , Lambert, H., Cross, N. L . , Overshreet, J . W.: Alteration of human sperm surface during in-vitro capacitation as assessed by lectin induced agglutination. Gamete Res., (1985); i2: 291-299.
  • Sinowatz, F., Friess, A. E . : Localisation of lectin receptors on bovine cpididymal spermatozoa using a colloidal gold techniques. Histochemistry, (1983); 79: 335-344.
  • Sinowatz, F., Volgmayer, J . K., Gabius, H. J . , Friess, A. E . : Cytochcmical analysis o f mammalian sperm membranes. Prog. Histoch. Cytoch., (1989); 19 (4): 1-74.
  • Spicer, S. S.: Advantages of histochemistry for the study of cell biology. Histochcmical Journal., (1993); 25: 533-547.
  • Tulsiani, D. R. P., Nagdas, S. K., Skudlarek, M. D., Orgebin-Crist, M - C : Rat sperm plasma membrane mannosidasc: Localisation and evidence for proteolytic processing during epididymal maturation. Dev. Biol., (1995); 167: 584-595.
Year 2009, Volume: 35 Issue: 2, 1 - 12, 20.11.2012

Abstract

References

  • Arya, M., Vanha-Perttula, T.: Lectin binding pattern of bull testis and epididymis. J. Androl.,(1985a);6: 230-242.
  • Bedford, J . M.: Maturation, transport & fate of spermatozoa in the epididymis. Handbook of physiology, Vol. V., Section-6, (cd.) Hamilton, D.W. & Green, R. O. Am. Phy. Soc, Washington D.C., (1975); 307-317.
  • Bernal, A., Torres, J . , Reyes, A., Rosado, A.: Presence and regional distribution of sialyl transferase in the epididymis of the rat. Biol. Reprod., (1980); 23: 290-293.
  • Briz, M. D., Bond, S., Pinart, B., Egozcue, J . , Camps, R.: Comparative study of boar sperm coming from the caput, corpus and cauda regions of the epididymis. J. Androl., (1995); 16(2): 175-188.
  • Brooks, D. E.: Secretion of proteins and glycoproteins by the rat epididymis: regional differences, androgen dependence, and effects of protease inhibitors, procaine, and tunicamycin. Biol. Reprod., (1981); 25: 1091-1097.
  • Datta, U.: Bioactivc substance(s) from a marine mollusc Telcscopium telcscopium and its role on mammalian reproduction. Ph.D. Thesis. Jadavpur University, Kolkata, India. 2003.
  • Drevius, L . O.: Bull spermatozoa as osmometers. J. Reprod. Fertility., (1972); 28: 29-39.
  • Duncan, D. B.: Multiple range and multiple F test. Biometrics., (1955); 11: 1-42.
  • Frazier, W., Glaser, L . : Surface components and cell recognition. Annu. Rev. Biochem.. (1979); 48: 491-496.
  • Gabius, H-J.: Vertebrate lectins and their possible role in fertilization, development and tumor biology. ln-vitro., (1987); 1: 75-84.
  • Goldstein, I. J . , Hayes, C. E.: The lectins: carbohydrate binding proteins of plants and animals. Adr. Carhydr. Chem. Biochem., (1978); 35: l'27-340.
  • Green, D. P.: Mammalian fertilization as a biological machine: a working model for adhesion and fusion of sperm and oocyte. Human Reprod., (1993): 8: 91-96.
  • Gwatkin, R., Williams, D.: Receptor activity of the solubilized hampster and mouse zona pellucida before and after the zona reaction. J. Reprod. Fetil., (1976); 19: 55-59.
  • Hinton, B. T., Palladino, M. A.: Epididymal epithelium: its contribution to the formation of a luminal fluid microenvironment. Micros. Res. Tech., (1995); 30: 67-81.
  • Jeyendran, R. S., Vandervent, H. H., Perez-Paleac, Z. M., Crabo, B. G., Zanevld, L . J . D.: Development of an assay to assess the functional integrity of human sperm membrane and its relationship to other semen characteristics. J. Reprod. Fcrtil., (1984); 70: pp. 219ı 225.
  • Jones, R.: Membrane remodeling during sperm maturation in the epididymis. Oxford Reviews of Reproductive Biology, (1989); 1: 285-337. Gout Sperm Surface Alteration During Epididymal Maturation An Avaluation 11
  • Jones, R., Brown, C. R., Von Gios, K. I., Parker, M . G.: Hormonal regulation of protein synthesis in the rai epididymis. Characterization of androgen-dependent and testicular fluid- dependent proteins. Biochem. J., (1980); 188: 667-676.
  • Koehler, J. K.: Lectins as probes of the spermatozoan surface. Arch. Androl., (1981); 6: 197-217.
  • Kunz, A., Brown, D., Orci, L . : Appearance of helix pomatia lectin binding sites on podocytc plasma membrane during glomerular differentiation. A quantitivc analysis using the lectin-gold technique. Lab. Invest., (1984); 51 (3): 317-324.
  • Levine, N., Marsh, D. J.: Micro puncture studies of the electrochemical aspects of fluid and electrolyte transport in individual seminiferous tubules, the epididymis and the vas deferens in rats. J. Physiol., (1971); 213 (3): 557-570.
  • Lis, H., Sharon, IN.: Lectins as molecules and as tools. Ann. Rev. Biochem., (1986); 55: pp. 35-67.
  • L i u , H. W., L i n , Y. C , Chao, C. F., Chang, S. Y., Sun, G. H . : GP-83 and GP-39, two glycoprotein secreted by human epididymis are conjugated to spermatozoa during maturation. Mol Human Reprod., (2000); 6 (5): 422-428.
  • Lopez, M . L . , deSouza. W., Bustos-Obregon, E.: C>tochemical analysis o f the anionic sites on the membrane o f the stallion spermatozoa during the epididymal transit. Gamete Res., (19S9); 18: pp.319-332.
  • Lowry, O. I L , Rosebrough, N . J., Farr, A. 1., Randall, R. J.: Protein measurement with the folin-phenol reagent. J. Biochem., (1951); 193, 265.
  • Mladenovic, L, Hajducovic. L.. Genbacev, O., Cuperlovic, M . , Movsesijan, M . : Lectin binding as a biological test in vitro for the prediction of functional activity of human spermatozoa. Gamete Res., (1993); 24: 403-413.
  • Monsigny, M . , Roche, A. C Kirnda. C , Midoux, P., Obernovitch, A.: Characterization and biological implications o f membrane lectins in tumors, lyphoid and myeloid cells. Biochem., (1988); 70: 1633-1649.
  • Moore, H . D. M . : Contribution of epididymal factors to sperm maturation and storage. Andrologia., (1998); 30: 233-239.
  • M vies, D. G.: Molecular mechanisms of sperm-egg membrane binding and fusion in mammals. Dev. Biol., (1993); ¡58: 35-45.
  • Nicolson, G. L . : The interactions of lectins with animal cell surfaces. Int. Rev. Cytol., (1974); 39:90-190.
  • Pakrashi, A., Datta, U.: in-vitro sperm agglutination and spermicidal activity o f protein isolated from a marine mollusc Telescopium telescopium (Gastropod). Indian J. Marine Sci., (2001); 30: 93-97.
  • Peleg, B. A., Ian Consscu, M . : Sperm agglutination and sperm absorption due to mixoviruses. Nature., ( 1966); 211:1211-1212.
  • Sanz, I . , Calvete, J. J., Mann, K., Gabius, H. J., Topfer-petersen, E.: Isolation and biochemical characterization of heparin binding protein from boar seminal plasma a dual role for sperm adhesion in fertilization. Mol. Reprod. Dev., (1993); 34: 37-43.
  • Sarkar, M . , Mazurndar, G. C , Chatterjee, T.: Goat sperm membrane: Lectin binding sites of sperm surface and lectin affinity chromatography o f the mature sperm membrane antigens. Biochion. Biophys. Acta., ( 1991); 1070(1); 19S-204.
  • Manik Lai HEMBRAM-Uttam D ATT A-Raj u DASGUPTA
  • Schwarz, M. A., Koehler, J . K.: Alteration in lectin binding to guineapig spermatozoa accompanying in vitro capacitation and acrosomc reaction. Biol. Reproduction, (1979); 21:1295-1299.
  • Serrano, H., Díaz-Esparza, L . , Garcia-Suarez, D.: Pig sperm membrane integrity evaluated by lectin labeling. Arch. Androl., (2001); 47 (1): 59-65.
  • Signer, S. L . , Lambert, H., Cross, N. L . , Overshreet, J . W.: Alteration of human sperm surface during in-vitro capacitation as assessed by lectin induced agglutination. Gamete Res., (1985); i2: 291-299.
  • Sinowatz, F., Friess, A. E . : Localisation of lectin receptors on bovine cpididymal spermatozoa using a colloidal gold techniques. Histochemistry, (1983); 79: 335-344.
  • Sinowatz, F., Volgmayer, J . K., Gabius, H. J . , Friess, A. E . : Cytochcmical analysis o f mammalian sperm membranes. Prog. Histoch. Cytoch., (1989); 19 (4): 1-74.
  • Spicer, S. S.: Advantages of histochemistry for the study of cell biology. Histochcmical Journal., (1993); 25: 533-547.
  • Tulsiani, D. R. P., Nagdas, S. K., Skudlarek, M. D., Orgebin-Crist, M - C : Rat sperm plasma membrane mannosidasc: Localisation and evidence for proteolytic processing during epididymal maturation. Dev. Biol., (1995); 167: 584-595.
There are 41 citations in total.

Details

Primary Language English
Journal Section Research Article
Authors

Manik Hembram This is me

Uttam Datta This is me

Raju Dasgupta This is me

Publication Date November 20, 2012
Published in Issue Year 2009 Volume: 35 Issue: 2

Cite

APA Hembram, M., Datta, U., & Dasgupta, R. (2012). GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, 35(2), 1-12. https://doi.org/10.16988/iuvfd.79065
AMA Hembram M, Datta U, Dasgupta R. GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM. iuvfd. November 2012;35(2):1-12. doi:10.16988/iuvfd.79065
Chicago Hembram, Manik, Uttam Datta, and Raju Dasgupta. “GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 35, no. 2 (November 2012): 1-12. https://doi.org/10.16988/iuvfd.79065.
EndNote Hembram M, Datta U, Dasgupta R (November 1, 2012) GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 35 2 1–12.
IEEE M. Hembram, U. Datta, and R. Dasgupta, “GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM”, iuvfd, vol. 35, no. 2, pp. 1–12, 2012, doi: 10.16988/iuvfd.79065.
ISNAD Hembram, Manik et al. “GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 35/2 (November 2012), 1-12. https://doi.org/10.16988/iuvfd.79065.
JAMA Hembram M, Datta U, Dasgupta R. GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM. iuvfd. 2012;35:1–12.
MLA Hembram, Manik et al. “GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, vol. 35, no. 2, 2012, pp. 1-12, doi:10.16988/iuvfd.79065.
Vancouver Hembram M, Datta U, Dasgupta R. GOAT SPERM SURFACE ALTERATION DURING EPIDIDYMAL MATURATION: AN EVALUATION BY MARINE BIOACTIVE COMPOUND FROM TELESCOPIUM TELESCOPIUM. iuvfd. 2012;35(2):1-12.