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Volumn 58, Issue 2, 2011, Pages 171-177

Zinc-binding proteins from boar seminal plasma-isolation, biochemical characteristics and influence on spermatozoa stored at 4 °C

Author keywords

Boar; Cold shock; Spermatozoa; Zinc; Zn 2+ binding proteins

Indexed keywords

CARRIER PROTEIN; ZINC;

EID: 79960137252     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (24)

References (64)
  • 1
    • 0028065724 scopus 로고
    • Low molecular weight components in bovine semen diffusate and their effects on sperm motility of bull sperm
    • Al-Somai N, Vishwanath R, Schannon P, Molan PC (1994) Low molecular weight components in bovine semen diffusate and their effects on sperm motility of bull sperm. Reprod Fertil Dev 6: 165-171.
    • (1994) Reprod Fertil Dev , vol.6 , pp. 165-171
    • Al-Somai, N.1    Vishwanath, R.2    Schannon, P.3    Molan, P.C.4
  • 3
    • 0013769988 scopus 로고
    • Estimation of molecular weight of proteins by Sephadex gel filtration
    • Andrews P (1964) Estimation of molecular weight of proteins by Sephadex gel filtration. Biochemistry 91: 222-227.
    • (1964) Biochemistry , vol.91 , pp. 222-227
    • Andrews, P.1
  • 5
    • 0019860989 scopus 로고
    • A critical physiological role of zinc in the structure and function of biomembranes
    • Bettger WJ, O'Dell BL (1981) A critical physiological role of zinc in the structure and function of biomembranes. Life Sci 28: 1425-1432.
    • (1981) Life Sci , vol.28 , pp. 1425-1432
    • Bettger, W.J.1    O'Dell, B.L.2
  • 7
    • 77649200040 scopus 로고    scopus 로고
    • Human sperm chromatin stabilization: a proposed model including zinc bridges
    • Bjorndahl L and Kvist U (2010) Human sperm chromatin stabilization: a proposed model including zinc bridges. Mol Hum Reprod 16: 23-29.
    • (2010) Mol Hum Reprod , vol.16 , pp. 23-29
    • Bjorndahl, L.1    Kvist, U.2
  • 8
    • 79960120407 scopus 로고
    • Cysteine interacts with a zinc dependent chromatin stability in epididymal boar spermatozoa
    • eds BD Bavister, J Cummins, ERS Rolan, Serono Symposium, Norwell, MA, USA
    • Bjorndahl L, Kvist U, Rodriguez H, Ploen L (1990) Cysteine interacts with a zinc dependent chromatin stability in epididymal boar spermatozoa. Fertilization in mammals. pp 416. eds BD Bavister, J Cummins, ERS Rolan, Serono Symposium, Norwell, MA, USA.
    • (1990) Fertilization in mammals , pp. 416
    • Bjorndahl, L.1    Kvist, U.2    Rodriguez, H.3    Ploen, L.4
  • 9
    • 0025810334 scopus 로고
    • Ejaculatory sequence in men with low sperm-chromatin-zinc
    • Bjorndahl L, Kjelberg S, Kvist U (1991) Ejaculatory sequence in men with low sperm-chromatin-zinc. Int J Androl 14: 174-178.
    • (1991) Int J Androl , vol.14 , pp. 174-178
    • Bjorndahl, L.1    Kjelberg, S.2    Kvist, U.3
  • 10
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P, Beckmann G (1993) The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 231: 539-545.
    • (1993) J Mol Biol , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 11
    • 0033213244 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility
    • Brandon CI, Heusner G, Caudle AB, Fayrer-Hosken R (1999) Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology 52: 863-873.
    • (1999) Theriogenology , vol.52 , pp. 863-873
    • Brandon, C.I.1    Heusner, G.2    Caudle, A.B.3    Fayrer-Hosken, R.4
  • 13
    • 0031589138 scopus 로고    scopus 로고
    • Isolation and characterization of heparin and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1
    • Calvete JJ, Raida M, Gentzel M, Urbanke C, Sanz L, Töpfer-Petersen E (1997) Isolation and characterization of heparin and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1. FEBS Lett 407: 201-206.
    • (1997) FEBS Lett , vol.407 , pp. 201-206
    • Calvete, J.J.1    Raida, M.2    Gentzel, M.3    Urbanke, C.4    Sanz, L.5    Töpfer-Petersen, E.6
  • 15
    • 80051720080 scopus 로고    scopus 로고
    • Motility stimulant effects of prostasome inclusion in swim-up medium on cryopreserved human spermatozoa
    • Carlsson L, Ronquist G, Stridsberg M, Johansson L (1997) Motility stimulant effects of prostasome inclusion in swim-up medium on cryopreserved human spermatozoa. Arch Androl 38: 215-221.
    • (1997) Arch Androl , vol.38 , pp. 215-221
    • Carlsson, L.1    Ronquist, G.2    Stridsberg, M.3    Johansson, L.4
  • 18
    • 78651153791 scopus 로고
    • Disc electrophoresis. Method and application to human serum proteins
    • Davis BJ (1964) Disc electrophoresis. Method and application to human serum proteins. Ann NY Acad Sci 121: 404-427.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 19
    • 33846582018 scopus 로고    scopus 로고
    • Semenogelin, the main protein of the human semen coagulum, regulates sperm function
    • De Lamirande E (2007) Semenogelin, the main protein of the human semen coagulum, regulates sperm function. Semin Thromb Hemost 33: 60-68.
    • (2007) Semin Thromb Hemost , vol.33 , pp. 60-68
    • De Lamirande, E.1
  • 20
    • 0034940268 scopus 로고    scopus 로고
    • Semenogelin, the main protein of semen coagulum, inhibits human sperm capacitation by interfering with the superoxide anion generated during this process
    • De Lamirande E, Yoshida K, Yoshiike M, Iwamoto T, Gagnon C (2001) Semenogelin, the main protein of semen coagulum, inhibits human sperm capacitation by interfering with the superoxide anion generated during this process. J Androl 22: 672-679.
    • (2001) J Androl , vol.22 , pp. 672-679
    • De Lamirande, E.1    Yoshida, K.2    Yoshiike, M.3    Iwamoto, T.4    Gagnon, C.5
  • 21
    • 0025265334 scopus 로고
    • Cold-induced ultrastructural changes in bull and boar sperm plasma membranes
    • De Leeuw FE, Chen HC, Colenbrander B, Verkleij A (1990) Cold-induced ultrastructural changes in bull and boar sperm plasma membranes. Cryobiology 27: 171-183.
    • (1990) Cryobiology , vol.27 , pp. 171-183
    • De Leeuw, F.E.1    Chen, H.C.2    Colenbrander, B.3    Verkleij, A.4
  • 22
    • 51549086806 scopus 로고    scopus 로고
    • The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins
    • Edstrom AML, Malm J, Frohm B, Martellini JA, Giwercman A, Morgelin M, Cole AM, Sorensen OE (2008) The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins. J Immunol 181: 3413-3421.
    • (2008) J Immunol , vol.181 , pp. 3413-3421
    • Edstrom, A.M.L.1    Malm, J.2    Frohm, B.3    Martellini, J.A.4    Giwercman, A.5    Morgelin, M.6    Cole, A.M.7    Sorensen, O.E.8
  • 23
    • 79952773159 scopus 로고    scopus 로고
    • Relationships between seminal plasma proteins and boar fertility
    • Flowers WL (2001) Relationships between seminal plasma proteins and boar fertility. Ann Swine Rep pp 1-4.
    • (2001) Ann Swine Rep , pp. 1-4
    • Flowers, W.L.1
  • 24
    • 0036045089 scopus 로고    scopus 로고
    • Fluorometric assessment of viability and mitochondrial status of boar spermatozoa following liquid storage
    • Fraser L, Lecewicz M, Strzeżek J (2002) Fluorometric assessment of viability and mitochondrial status of boar spermatozoa following liquid storage. Polish J Vet Sci 5: 85-92.
    • (2002) Polish J Vet Sci , vol.5 , pp. 85-92
    • Fraser, L.1    Lecewicz, M.2    Strzezek, J.3
  • 25
    • 4544225278 scopus 로고    scopus 로고
    • A comprehensive characterization of the peptide and protein constituents of human seminal fluid
    • Fung KYC, Glode M, Green S, Duncan MW (2004) A comprehensive characterization of the peptide and protein constituents of human seminal fluid. Prostate 61: 171-181.
    • (2004) Prostate , vol.61 , pp. 171-181
    • Fung, K.Y.C.1    Glode, M.2    Green, S.3    Duncan, M.W.4
  • 26
    • 18844430042 scopus 로고    scopus 로고
    • Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles
    • Gatti JL, Metayer S, Belghazi M, Dacheux F, Dacheux JL (2005) Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles. Biol Reprod 72: 1452-1465.
    • (2005) Biol Reprod , vol.72 , pp. 1452-1465
    • Gatti, J.L.1    Metayer, S.2    Belghazi, M.3    Dacheux, F.4    Dacheux, J.L.5
  • 27
    • 0344934925 scopus 로고
    • Nature of large antibacterial proteins in bovine seminal plasma formed by reversible aggregation
    • Hameed I, Molan P, Shannon P (1991) Nature of large antibacterial proteins in bovine seminal plasma formed by reversible aggregation. NZJ Agric Res 34: 467-470.
    • (1991) NZJ Agric Res , vol.34 , pp. 467-470
    • Hameed, I.1    Molan, P.2    Shannon, P.3
  • 28
    • 0033151687 scopus 로고    scopus 로고
    • Relevance of zinc in human sperm flagella and its relation to motility
    • Henkel R, Bittner J, Weber R, Huther F, Miska W (1999) Relevance of zinc in human sperm flagella and its relation to motility. Fertil Steril 71: 1138-1143.
    • (1999) Fertil Steril , vol.71 , pp. 1138-1143
    • Henkel, R.1    Bittner, J.2    Weber, R.3    Huther, F.4    Miska, W.5
  • 29
    • 0037386902 scopus 로고    scopus 로고
    • Resorption of the element zinc from spermatozoa by the epididymal epithelium
    • Henkel R, Bladauf Ch, Schill WB (2003) Resorption of the element zinc from spermatozoa by the epididymal epithelium. Reprod Dom Anim 38: 97-101.
    • (2003) Reprod Dom Anim , vol.38 , pp. 97-101
    • Henkel, R.1    Bladauf, C.2    Schill, W.B.3
  • 30
    • 34548643538 scopus 로고    scopus 로고
    • Cryosurvival and in vitro fertilizing capacity postthaw is improved when boar spermatozoa are frozen in the presence of seminal plasma from good freezer boars
    • Hernandez M, Roca J, Calvete JJ, Sanz L, Muinc-Blanco T, Cebrian-Perez JA, Vazquez JM, Martinez EA (2007) Cryosurvival and in vitro fertilizing capacity postthaw is improved when boar spermatozoa are frozen in the presence of seminal plasma from good freezer boars. J Androl 5: 689-697.
    • (2007) J Androl , vol.5 , pp. 689-697
    • Hernandez, M.1    Roca, J.2    Calvete, J.J.3    Sanz, L.4    Muinc-Blanco, T.5    Cebrian-Perez, J.A.6    Vazquez, J.M.7    Martinez, E.A.8
  • 31
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven J, Dernick R (1985) Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6: 103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 32
    • 0033288939 scopus 로고    scopus 로고
    • 2+-binding proteins from boar seminal plasma
    • 2+-binding proteins from boar seminal plasma. Acta Biochim Pol 46: 935-939.
    • (1999) Acta Biochim Pol , vol.46 , pp. 935-939
    • Hołody, D.1    Strzezek, J.2
  • 34
    • 0347657532 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability
    • Jobim MIM, Oberst ER, Salbego CG, Souza DO, Wald VB, Tramontina F, Mattos RC (2004) Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability. Theriogenology 61: 255-266.
    • (2004) Theriogenology , vol.61 , pp. 255-266
    • Jobim, M.I.M.1    Oberst, E.R.2    Salbego, C.G.3    Souza, D.O.4    Wald, V.B.5    Tramontina, F.6    Mattos, R.C.7
  • 35
    • 1942454415 scopus 로고    scopus 로고
    • Boar seminal plasma proteins and their binding properties. A review
    • Jonakova V, Ticha M (2004) Boar seminal plasma proteins and their binding properties. A review. Collect Czech Chem Commun 69: 461-475.
    • (2004) Collect Czech Chem Commun , vol.69 , pp. 461-475
    • Jonakova, V.1    Ticha, M.2
  • 36
    • 17644419655 scopus 로고    scopus 로고
    • Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen
    • Jonsson M, Linse S, Frohm B, Lundwall A, Malm J (2005) Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen. Biochem J 387: 447-453.
    • (2005) Biochem J , vol.387 , pp. 447-453
    • Jonsson, M.1    Linse, S.2    Frohm, B.3    Lundwall, A.4    Malm, J.5
  • 38
    • 0027493349 scopus 로고
    • Fertility-associated proteins in Holstein bull seminal plasma
    • Killian GJ, Chapman DA, Rogowski LA (1993) Fertility-associated proteins in Holstein bull seminal plasma. Biol Reprod 49: 1202-1207.
    • (1993) Biol Reprod , vol.49 , pp. 1202-1207
    • Killian, G.J.1    Chapman, D.A.2    Rogowski, L.A.3
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 0033814795 scopus 로고    scopus 로고
    • Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specifity and regulation by Zn(2+), a tight-binding inhibitor
    • Malm J, Hellman J, Hogg P, Lilja H (2000) Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specifity and regulation by Zn(2+), a tight-binding inhibitor. Prostate 45: 132-139.
    • (2000) Prostate , vol.45 , pp. 132-139
    • Malm, J.1    Hellman, J.2    Hogg, P.3    Lilja, H.4
  • 43
    • 33750688276 scopus 로고    scopus 로고
    • Effects of bovine serum albumin and trehalose in semen diluents for improvement of frozen thawed ram spermatozoa
    • Matsuoka T, Imai H, Kohno H, Fukui Y (2006) Effects of bovine serum albumin and trehalose in semen diluents for improvement of frozen thawed ram spermatozoa. J Reprod. Dev. 52: 675-683.
    • (2006) J Reprod. Dev. , vol.52 , pp. 675-683
    • Matsuoka, T.1    Imai, H.2    Kohno, H.3    Fukui, Y.4
  • 44
    • 77649305726 scopus 로고    scopus 로고
    • In vitro antioxidant activity of the prostatic secretory granules in rabbit semen after exposure to organic peroxides
    • Mourvaki E, Cardinali R, Dal Bosco A, Castellini C (2010) In vitro antioxidant activity of the prostatic secretory granules in rabbit semen after exposure to organic peroxides. Biol Reprod Endocrinol 8: 16-23.
    • (2010) Biol Reprod Endocrinol , vol.8 , pp. 16-23
    • Mourvaki, E.1    Cardinali, R.2    Dal Bosco, A.3    Castellini, C.4
  • 45
    • 33746891731 scopus 로고
    • High resolution of two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PZ, Goodman HM, O'Farrell PH (1977) High resolution of two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12: 113-142.
    • (1977) Cell , vol.12 , pp. 113-142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 46
    • 33645876205 scopus 로고    scopus 로고
    • Biochemical characterization and membrane fluidity of membranous vesicles isolated from boar seminal plasma
    • Piehl LL, Cisale H, Torres N, Capani F, Sterin-Speziale N, Hager A (2006) Biochemical characterization and membrane fluidity of membranous vesicles isolated from boar seminal plasma. Anim Reprod Sci 92: 401-410.
    • (2006) Anim Reprod Sci , vol.92 , pp. 401-410
    • Piehl, L.L.1    Cisale, H.2    Torres, N.3    Capani, F.4    Sterin-Speziale, N.5    Hager, A.6
  • 47
    • 0036538366 scopus 로고    scopus 로고
    • Design of new and sensitive fluorogenic substrates for human kallikrein hK3 (prostate-specific antigen) derived from semenogelin sequences
    • Rehault S, Brillard-Bourdet M, Bourgeois L, Frenette G, Juliano L, Gauthier F, Moreau T (2002) Design of new and sensitive fluorogenic substrates for human kallikrein hK3 (prostate-specific antigen) derived from semenogelin sequences. Biochim Biophys Acta 1596: 55-62.
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 55-62
    • Rehault, S.1    Brillard-Bourdet, M.2    Bourgeois, L.3    Frenette, G.4    Juliano, L.5    Gauthier, F.6    Moreau, T.7
  • 48
    • 0033016106 scopus 로고    scopus 로고
    • Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein
    • Robert M, Gagnon C (1999) Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein. Cell Mol Life Sci 55: 944 -960.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 944-960
    • Robert, M.1    Gagnon, C.2
  • 50
    • 0022257512 scopus 로고
    • The prostasome: its secretion and function in man
    • Ronquist G, Brody I (1985) The prostasome: its secretion and function in man. Biochim Biophys Acta 822: 203-218.
    • (1985) Biochim Biophys Acta , vol.822 , pp. 203-218
    • Ronquist, G.1    Brody, I.2
  • 52
    • 0031828567 scopus 로고    scopus 로고
    • Antioxidant capacity of prostasomes in human semen
    • Saez F, Motta C, Boucher D, Grizard G (1998) Antioxidant capacity of prostasomes in human semen. Mol Hum Reprod 4: 667-672.
    • (1998) Mol Hum Reprod , vol.4 , pp. 667-672
    • Saez, F.1    Motta, C.2    Boucher, D.3    Grizard, G.4
  • 54
    • 0012844979 scopus 로고
    • Cationic peptides obtained by reversible disaggregation of antibacterial proteins of bovine seminal plasma
    • Shannon P, Curson B, Molan PC (1987) Cationic peptides obtained by reversible disaggregation of antibacterial proteins of bovine seminal plasma. NZJ Agric Res 30: 195-202.
    • (1987) NZJ Agric Res , vol.30 , pp. 195-202
    • Shannon, P.1    Curson, B.2    Molan, P.C.3
  • 55
    • 40749112313 scopus 로고    scopus 로고
    • Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa
    • Siciliano L, Marciano V, Caprino A (2008) Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa. Reprod Biol Endocrinol 6: 5-10.
    • (2008) Reprod Biol Endocrinol , vol.6 , pp. 5-10
    • Siciliano, L.1    Marciano, V.2    Caprino, A.3
  • 56
    • 84907133778 scopus 로고
    • Zinc uptake in human seminal spermatozoa: characterization and effects on cell membranes
    • Silverstroni L, Menditto A, Modesti A, Scarpa S (1989) Zinc uptake in human seminal spermatozoa: characterization and effects on cell membranes. Arch Androl 23: 97-103.
    • (1989) Arch Androl , vol.23 , pp. 97-103
    • Silverstroni, L.1    Menditto, A.2    Modesti, A.3    Scarpa, S.4
  • 57
    • 0347126564 scopus 로고    scopus 로고
    • Seminal plasma and some biological functions of spermatozoa
    • Strzeżek J (1999) Seminal plasma and some biological functions of spermatozoa. Adv Cell Biol 26: 59-68.
    • (1999) Adv Cell Biol , vol.26 , pp. 59-68
    • Strzezek, J.1
  • 58
    • 0344246779 scopus 로고
    • Zinc ion-dependent protein in boar semen. I. Egg yolk precipitating activity and some biochemical properties
    • Strzeżek J, Hopfer E (1987) Zinc ion-dependent protein in boar semen. I. Egg yolk precipitating activity and some biochemical properties. Anim Reprod Sci 13: 117-131.
    • (1987) Anim Reprod Sci , vol.13 , pp. 117-131
    • Strzezek, J.1    Hopfer, E.2
  • 59
    • 0345109141 scopus 로고
    • Zinc-ion dependent protein in boar semen. II. Effects on sperm motility and antibacterial properties
    • Strzeżek J, Hopfer E, Zaborniak A (1987) Zinc-ion dependent protein in boar semen. II. Effects on sperm motility and antibacterial properties. Anim Reprod Sci 13: 133-142.
    • (1987) Anim Reprod Sci , vol.13 , pp. 133-142
    • Strzezek, J.1    Hopfer, E.2    Zaborniak, A.3
  • 60
    • 13444252667 scopus 로고    scopus 로고
    • Effect of bovine serum albumine on freezing of canine semen
    • Uysal O, Korkmaz T, Tosun H (2005) Effect of bovine serum albumine on freezing of canine semen. Indian Vet J 82: 97-98.
    • (2005) Indian Vet J , vol.82 , pp. 97-98
    • Uysal, O.1    Korkmaz, T.2    Tosun, H.3
  • 62
    • 0016843679 scopus 로고
    • Use of a Giemsa stain to detect changes in acrosomes of frozen ram spermatozoa
    • Watson PF (1975) Use of a Giemsa stain to detect changes in acrosomes of frozen ram spermatozoa. Vet Rec 1: 12-15.
    • (1975) Vet Rec , vol.1 , pp. 12-15
    • Watson, P.F.1
  • 63
    • 40949124276 scopus 로고    scopus 로고
    • Physiological roles of semenogelin I and zinc in sperm motility and semen coagulation on ejaculation in humans
    • Yoshida K, Kawano N, Yoshiike M, Yoshida M, Iwamoto T, Morisawa M (2008) Physiological roles of semenogelin I and zinc in sperm motility and semen coagulation on ejaculation in humans. MHRBasic Sci Reprod Med 3: 151-156.
    • (2008) MHRBasic Sci Reprod Med , vol.3 , pp. 151-156
    • Yoshida, K.1    Kawano, N.2    Yoshiike, M.3    Yoshida, M.4    Iwamoto, T.5    Morisawa, M.6
  • 64
    • 0027428574 scopus 로고
    • The abundant 19-kilodalton protein associated with human sperm nuclei that is related to seminal plasma alpha-inhibin
    • Zalensky AO, Yau P, Brenerman JW, Bradbury EM (1993) The abundant 19-kilodalton protein associated with human sperm nuclei that is related to seminal plasma alpha-inhibin. Mol Reprod Dev 36:164-173.
    • (1993) Mol Reprod Dev , vol.36 , pp. 164-173
    • Zalensky, A.O.1    Yau, P.2    Brenerman, J.W.3    Bradbury, E.M.4


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