메뉴 건너뛰기




Volumn 274, Issue 20, 2007, Pages 5390-5405

Recombinant bovine zona pellucida glycoproteins ZP3 and ZP4 coexpressed in Sf9 cells form a sperm-binding active hetero-complex

Author keywords

Baculovirus Sf9; Fertilization; Glycoprotein; Zona pellucida; ZP domain

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN ZP33; GLYCOPROTEIN ZP34; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34848826611     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06065.x     Document Type: Article
Times cited : (23)

References (56)
  • 1
    • 2442754050 scopus 로고    scopus 로고
    • Carbohydrate-based interactions on the route of a spermatozoon to fertilization
    • Töpfer-Petersen E (1999) Carbohydrate-based interactions on the route of a spermatozoon to fertilization. Hum Reprod Update 5, 314 329.
    • (1999) Hum Reprod Update , vol.5 , pp. 314-329
    • Töpfer-Petersen, E.1
  • 3
    • 1842843784 scopus 로고    scopus 로고
    • Insights into the molecular basis of sperm-egg recognition in mammals
    • Hoodbhoy T Dean J (2004) Insights into the molecular basis of sperm-egg recognition in mammals. Reproduction 127, 417 422.
    • (2004) Reproduction , vol.127 , pp. 417-422
    • Hoodbhoy, T.1    Dean, J.2
  • 5
    • 16844387092 scopus 로고    scopus 로고
    • Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins
    • Hoodbhoy T, Joshi S, Boja ES, Williams SA, Stanley P Dean J (2005) Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins. J Biol Chem 280, 12721 12731.
    • (2005) J Biol Chem , vol.280 , pp. 12721-12731
    • Hoodbhoy, T.1    Joshi, S.2    Boja, E.S.3    Williams, S.A.4    Stanley, P.5    Dean, J.6
  • 6
    • 0028045713 scopus 로고
    • Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: The ZPA, ZPB and ZPC gene families
    • Harris JD, Hibler DW, Fontenot GK, Hsu KT, Yurewicz EC Sacco AG (1994) Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families. DNA Seq 4, 361 393.
    • (1994) DNA Seq , vol.4 , pp. 361-393
    • Harris, J.D.1    Hibler, D.W.2    Fontenot, G.K.3    Hsu, K.T.4    Yurewicz, E.C.5    Sacco, A.G.6
  • 7
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida
    • Bleil JD Wassarman PM (1980) Structure and function of the zona pellucida: identification and characterization of the proteins of the mouse oocyte's zona pellucida. Dev Biol 76, 185 202.
    • (1980) Dev Biol , vol.76 , pp. 185-202
    • Bleil, J.D.1    Wassarman, P.M.2
  • 8
    • 0032719660 scopus 로고    scopus 로고
    • Identification of the true human orthologue of the mouse Zp1 gene: Evidence for greater complexity in the mammalian zona pellucida?
    • Hughes DC Barratt CLR (1999) Identification of the true human orthologue of the mouse Zp1 gene: evidence for greater complexity in the mammalian zona pellucida? Biochim Biophys Acta 1447, 303 306.
    • (1999) Biochim Biophys Acta , vol.1447 , pp. 303-306
    • Hughes, D.C.1    Barratt, C.L.R.2
  • 10
    • 0036307181 scopus 로고    scopus 로고
    • The ZP domain is a conserved module for polymerization of extracellular proteins
    • Jovine L, Qi H, Williams Z, Litscher E Wassarman PM (2002) The ZP domain is a conserved module for polymerization of extracellular proteins. Nat Cell Biol 4, 457 461.
    • (2002) Nat Cell Biol , vol.4 , pp. 457-461
    • Jovine, L.1    Qi, H.2    Williams, Z.3    Litscher, E.4    Wassarman, P.M.5
  • 12
    • 0029060459 scopus 로고
    • Coordinate expression of the three zona pellucida genes during mouse oogenesis
    • Epifano O, Liang LF, Familari M, Moos MC Jr. Dean J (1995) Coordinate expression of the three zona pellucida genes during mouse oogenesis. Development 121, 1947 1956.
    • (1995) Development , vol.121 , pp. 1947-1956
    • Epifano, O.1    Liang, L.F.2    Familari, M.3    Moos Jr., M.C.4    Dean, J.5
  • 13
    • 0022429080 scopus 로고
    • Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat
    • Greve JM Wassarman PM (1985) Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat. J Mol Biol 181, 253 264.
    • (1985) J Mol Biol , vol.181 , pp. 253-264
    • Greve, J.M.1    Wassarman, P.M.2
  • 14
    • 0030333226 scopus 로고    scopus 로고
    • Structure and function of the N-linked carbohydrate chains of pig zona pellucida glycoproteins
    • Nakano M, Yonezawa N, Hatanaka Y Noguchi S (1996) Structure and function of the N-linked carbohydrate chains of pig zona pellucida glycoproteins. J Reprod Fertil Suppl 50, 25 34.
    • (1996) J Reprod Fertil Suppl , vol.50 , pp. 25-34
    • Nakano, M.1    Yonezawa, N.2    Hatanaka, Y.3    Noguchi, S.4
  • 15
    • 0032571326 scopus 로고    scopus 로고
    • Hetero-oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles
    • Yurewicz EC, Sacco AG, Gupta SK, Xu N Gage DA (1998) Hetero- oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles. J Biol Chem 273, 7488 7494.
    • (1998) J Biol Chem , vol.273 , pp. 7488-7494
    • Yurewicz, E.C.1    Sacco, A.G.2    Gupta, S.K.3    Xu, N.4    Gage, D.A.5
  • 18
    • 0032703522 scopus 로고    scopus 로고
    • Disulfide formation in bovine zona pellucida glycoproteins during fertilization: Evidence for the involvement of cystine cross-linkages in hardening of the zona pellucida
    • Iwamoto K, Ikeda K, Yonezawa N, Noguchi S, Kudo K, Hamano S, Kuwayama M Nakano M (1999) Disulfide formation in bovine zona pellucida glycoproteins during fertilization: evidence for the involvement of cystine cross-linkages in hardening of the zona pellucida. J Reprod Fertil 117, 395 402.
    • (1999) J Reprod Fertil , vol.117 , pp. 395-402
    • Iwamoto, K.1    Ikeda, K.2    Yonezawa, N.3    Noguchi, S.4    Kudo, K.5    Hamano, S.6    Kuwayama, M.7    Nakano, M.8
  • 19
    • 0027171178 scopus 로고
    • Nucleotide sequence of cDNA encoding ZP3α, a sperm-binding glycoprotein from zona pellucida of pig oocyte
    • Yurewicz EC, Hibler D, Fontenot GK, Sacco AG Harris J (1993) Nucleotide sequence of cDNA encoding ZP3α, a sperm-binding glycoprotein from zona pellucida of pig oocyte. Biochim Biophys Acta 1174, 211 214.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 211-214
    • Yurewicz, E.C.1    Hibler, D.2    Fontenot, G.K.3    Sacco, A.G.4    Harris, J.5
  • 20
    • 0028985303 scopus 로고
    • Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization
    • Taya T, Yamasaki N, Tsubamoto H, Hasegawa A Koyama K (1995) Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization. Biochem Biophys Res Commun 207, 790 799.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 790-799
    • Taya, T.1    Yamasaki, N.2    Tsubamoto, H.3    Hasegawa, A.4    Koyama, K.5
  • 21
    • 0034819583 scopus 로고    scopus 로고
    • Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona
    • Yonezawa N, Fukui N, Kuno M, Shinoda M, Goko S, Mitsui S Nakano M (2001) Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona. Eur J Biochem 268, 3587 3594.
    • (2001) Eur J Biochem , vol.268 , pp. 3587-3594
    • Yonezawa, N.1    Fukui, N.2    Kuno, M.3    Shinoda, M.4    Goko, S.5    Mitsui, S.6    Nakano, M.7
  • 22
    • 0023164968 scopus 로고
    • Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of α- And β-glycoproteins following digestion of lactosaminoglycan with endo-β-galactosidase
    • Yurewicz EC, Sacco AG Subramanian MG (1987) Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of α- and β-glycoproteins following digestion of lactosaminoglycan with endo-β-galactosidase. J Biol Chem 262, 564 571.
    • (1987) J Biol Chem , vol.262 , pp. 564-571
    • Yurewicz, E.C.1    Sacco, A.G.2    Subramanian, M.G.3
  • 24
    • 0021874149 scopus 로고
    • O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity
    • Florman HM Wassarman PM (1985) O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell 41, 313 324.
    • (1985) Cell , vol.41 , pp. 313-324
    • Florman, H.M.1    Wassarman, P.M.2
  • 25
    • 0032568506 scopus 로고    scopus 로고
    • Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm
    • Chen J, Litscher ES Wassarman PM (1998) Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. Proc Natl Acad Sci USA 95, 6193 6197.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6193-6197
    • Chen, J.1    Litscher, E.S.2    Wassarman, P.M.3
  • 26
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida proteins using mass spectrometry
    • Boja ES, Hoodbhoy T, Fales HM Dean J (2003) Structural characterization of native mouse zona pellucida proteins using mass spectrometry. J Biol Chem 278, 34189 34202.
    • (2003) J Biol Chem , vol.278 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Dean, J.4
  • 27
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from β 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu Q Shur BD (1997) Sperm from β 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development 124, 4121 4131.
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 28
    • 7644233735 scopus 로고    scopus 로고
    • Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant
    • Shi S, Williams SA, Seppo A, Kurniawan H, Chen W, Ye Z, Marth DJ Stanley P (2004) Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. Mol Cell Biol 24, 9920 9929.
    • (2004) Mol Cell Biol , vol.24 , pp. 9920-9929
    • Shi, S.1    Williams, S.A.2    Seppo, A.3    Kurniawan, H.4    Chen, W.5    Ye, Z.6    Marth, D.J.7    Stanley, P.8
  • 29
    • 0028982258 scopus 로고
    • Oocyte Gal α 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall AD, Maly P Lowe JB (1995) Oocyte Gal α 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J Biol Chem 270, 21437 21440.
    • (1995) J Biol Chem , vol.270 , pp. 21437-21440
    • Thall, A.D.1    Maly, P.2    Lowe, J.B.3
  • 30
    • 0032521660 scopus 로고    scopus 로고
    • Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida
    • Kudo K, Yonezawa N, Katsumata T, Aoki H Nakano M (1998) Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida. Eur J Biochem 252, 492 499.
    • (1998) Eur J Biochem , vol.252 , pp. 492-499
    • Kudo, K.1    Yonezawa, N.2    Katsumata, T.3    Aoki, H.4    Nakano, M.5
  • 31
    • 0025984497 scopus 로고
    • Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins
    • Yurewicz EC, Pack BA Sacco AG (1991) Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins. Mol Reprod Dev 30, 126 134.
    • (1991) Mol Reprod Dev , vol.30 , pp. 126-134
    • Yurewicz, E.C.1    Pack, B.A.2    Sacco, A.G.3
  • 32
    • 11244311568 scopus 로고    scopus 로고
    • Participation of the nonreducing terminal β-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding
    • Yonezawa N, Amari S, Takahashi K, Ikeda K, Imai FL, Kanai S, Kikuchi K Nakano M (2005) Participation of the nonreducing terminal β-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding. Mol Reprod Dev 70, 222 227.
    • (2005) Mol Reprod Dev , vol.70 , pp. 222-227
    • Yonezawa, N.1    Amari, S.2    Takahashi, K.3    Ikeda, K.4    Imai, F.L.5    Kanai, S.6    Kikuchi, K.7    Nakano, M.8
  • 33
    • 0029830057 scopus 로고    scopus 로고
    • Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs
    • Katsumata T, Noguchi S, Yonezawa N, Tanokura M Nakano M (1996) Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs. Eur J Biochem 240, 448 453.
    • (1996) Eur J Biochem , vol.240 , pp. 448-453
    • Katsumata, T.1    Noguchi, S.2    Yonezawa, N.3    Tanokura, M.4    Nakano, M.5
  • 34
    • 0035040864 scopus 로고    scopus 로고
    • Essential role of the nonreducing terminal α-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm-egg binding
    • Amari S, Yonezawa N, Mitsui S, Katsumata T, Hamano S, Kuwayama M, Hashimoto Y, Suzuki A, Takeda Y Nakano M (2001) Essential role of the nonreducing terminal α-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm-egg binding. Mol Reprod Dev 59, 221 226.
    • (2001) Mol Reprod Dev , vol.59 , pp. 221-226
    • Amari, S.1    Yonezawa, N.2    Mitsui, S.3    Katsumata, T.4    Hamano, S.5    Kuwayama, M.6    Hashimoto, Y.7    Suzuki, A.8    Takeda, Y.9    Nakano, M.10
  • 35
    • 0038105489 scopus 로고    scopus 로고
    • Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC
    • Yonezawa N Nakano M (2003) Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC. Biochem Biophys Res Commun 307, 877 882.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 877-882
    • Yonezawa, N.1    Nakano, M.2
  • 36
    • 0035969977 scopus 로고    scopus 로고
    • Secretion of mouse ZP3, the sperm receptor, requires cleavage of its polypeptide at a consensus furin cleavage-site
    • Williams Z Wassarman PM (2001) Secretion of mouse ZP3, the sperm receptor, requires cleavage of its polypeptide at a consensus furin cleavage-site. Biochemistry 40, 929 937.
    • (2001) Biochemistry , vol.40 , pp. 929-937
    • Williams, Z.1    Wassarman, P.M.2
  • 37
    • 0036234958 scopus 로고    scopus 로고
    • Conserved furin cleavage site not essential for secretion and integration of ZP3 into the extracellular egg coat of transgenic mice
    • Zhao M, Gold L, Ginsberg AM, Liang LF Dean J (2002) Conserved furin cleavage site not essential for secretion and integration of ZP3 into the extracellular egg coat of transgenic mice. Mol Cell Biol 22, 3111 3120.
    • (2002) Mol Cell Biol , vol.22 , pp. 3111-3120
    • Zhao, M.1    Gold, L.2    Ginsberg, A.M.3    Liang, L.F.4    Dean, J.5
  • 38
    • 0036157586 scopus 로고    scopus 로고
    • Proteolytic processing of human zona pellucida proteins
    • Kiefer SM Saling P (2002) Proteolytic processing of human zona pellucida proteins. Biol Reprod 66, 407 414.
    • (2002) Biol Reprod , vol.66 , pp. 407-414
    • Kiefer, S.M.1    Saling, P.2
  • 39
    • 38149145468 scopus 로고
    • Assessing acrosomal status of bovine sperm using fluoresceinated lectins
    • Cross NL Watson SK (1994) Assessing acrosomal status of bovine sperm using fluoresceinated lectins. Theriogenology 42, 89 98.
    • (1994) Theriogenology , vol.42 , pp. 89-98
    • Cross, N.L.1    Watson, S.K.2
  • 40
    • 0036042540 scopus 로고    scopus 로고
    • Localization of N-linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida
    • Ikeda K, Yonezawa N, Naoi K, Katsumata T, Hamano S Nakano M (2002) Localization of N-linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida. Eur J Biochem 269, 4257 4266.
    • (2002) Eur J Biochem , vol.269 , pp. 4257-4266
    • Ikeda, K.1    Yonezawa, N.2    Naoi, K.3    Katsumata, T.4    Hamano, S.5    Nakano, M.6
  • 41
    • 0027381117 scopus 로고
    • Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation
    • Voss T, Ergulen E, Ahorn H, Kubelka V, Sugiyama K, Maurer-Fogy I Glossl J (1993) Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation. Eur J Biochem 217, 913 919.
    • (1993) Eur J Biochem , vol.217 , pp. 913-919
    • Voss, T.1    Ergulen, E.2    Ahorn, H.3    Kubelka, V.4    Sugiyama, K.5    Maurer-Fogy, I.6    Glossl, J.7
  • 42
  • 44
    • 0023715942 scopus 로고
    • The regulation of acrosomal exocytosis. I. Sperm capacitation is required for the induction of acrosomal reactions by the bovine zona pellucida in vitro
    • Florman HM First NL (1988) The regulation of acrosomal exocytosis. I. Sperm capacitation is required for the induction of acrosomal reactions by the bovine zona pellucida in vitro. Dev Biol 128, 453 463.
    • (1988) Dev Biol , vol.128 , pp. 453-463
    • Florman, H.M.1    First, N.L.2
  • 45
    • 0023708198 scopus 로고
    • Regulation of acrosomal exocytosis. II. the zona pellucida-induced acrosome reaction of bovine spermatozoa is controlled by extrinsic positive regulatory elements
    • Florman HM First NL (1988) Regulation of acrosomal exocytosis. II. The zona pellucida-induced acrosome reaction of bovine spermatozoa is controlled by extrinsic positive regulatory elements. Dev Biol 128, 464 473.
    • (1988) Dev Biol , vol.128 , pp. 464-473
    • Florman, H.M.1    First, N.L.2
  • 46
    • 34248587212 scopus 로고    scopus 로고
    • Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis
    • Baibakov B, Gauthier L, Talbot P, Rankin TL Dean J (2007) Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis. Development 134, 933 943.
    • (2007) Development , vol.134 , pp. 933-943
    • Baibakov, B.1    Gauthier, L.2    Talbot, P.3    Rankin, T.L.4    Dean, J.5
  • 47
    • 0028325798 scopus 로고
    • Amino acid sequence of a porcine zona pellucida glycoprotein ZP4 determined by peptide mapping and cDNA cloning
    • Hasegawa A, Koyama K, Okazaki Y, Sugimoto M Isojima S (1994) Amino acid sequence of a porcine zona pellucida glycoprotein ZP4 determined by peptide mapping and cDNA cloning. J Reprod Fertil 100, 245 255.
    • (1994) J Reprod Fertil , vol.100 , pp. 245-255
    • Hasegawa, A.1    Koyama, K.2    Okazaki, Y.3    Sugimoto, M.4    Isojima, S.5
  • 48
    • 0024515399 scopus 로고
    • Characterization of a proteinase that cleaves zona pellucida glycoprotein ZP2 following activation of mouse eggs
    • Moller CC Wassarman PM (1989) Characterization of a proteinase that cleaves zona pellucida glycoprotein ZP2 following activation of mouse eggs. Dev Biol 132, 103 112.
    • (1989) Dev Biol , vol.132 , pp. 103-112
    • Moller, C.C.1    Wassarman, P.M.2
  • 50
    • 0030949116 scopus 로고    scopus 로고
    • Rolling in the clover: Trefoil factor family (TFF)-domain peptides, cell migration and cancer
    • Wright NA, Hoffmann W, Otto WR, Rio MC Thim L (1997) Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer. FEBS Lett 408, 121 123.
    • (1997) FEBS Lett , vol.408 , pp. 121-123
    • Wright, N.A.1    Hoffmann, W.2    Otto, W.R.3    Rio, M.C.4    Thim, L.5
  • 52
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate- phenol-chloroform extraction
    • Chomczynski P Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate- phenol-chloroform extraction. Anal Biochem 162, 156 159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 53
    • 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
  • 54
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76, 4350 4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 55
    • 0016642448 scopus 로고
    • Capacitation of rabbit spermatozoa in vitro
    • Brackett BG Oliphant G (1975) Capacitation of rabbit spermatozoa in vitro. Biol Reprod 12, 260 274.
    • (1975) Biol Reprod , vol.12 , pp. 260-274
    • Brackett, B.G.1    Oliphant, G.2
  • 56
    • 0026607821 scopus 로고
    • Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida
    • Noguchi S, Hatanaka Y, Tobita T Nakano M (1992) Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida. Eur J Biochem 204, 1089 1100.
    • (1992) Eur J Biochem , vol.204 , pp. 1089-1100
    • Noguchi, S.1    Hatanaka, Y.2    Tobita, T.3    Nakano, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.