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Volumn 43, Issue 1, 2008, Pages 15-21

Identification of RSVP14 and RSVP20 components by two-dimensional electrophoresis and western-blotting

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHINE DERIVATIVE; SEMINAL PLASMA PROTEIN; SEMINAL VESICLE SECRETORY PROTEIN; TRI N BUTYLPHOSPHINE; TRI-N-BUTYLPHOSPHINE; UNCLASSIFIED DRUG;

EID: 38149072551     PISSN: 09366768     EISSN: 14390531     Source Type: Journal    
DOI: 10.1111/j.1439-0531.2006.00845.x     Document Type: Article
Times cited : (24)

References (43)
  • 3
    • 20544460230 scopus 로고    scopus 로고
    • Immunocytochemical localization and biochemical characterization of two seminal plasma proteins which protect ram spermatozoa against cold-shock
    • Barrios B, Fernández-Juan M, Muiño-Blanco T, Cebrián-Pérez JA, 2005 : Immunocytochemical localization and biochemical characterization of two seminal plasma proteins which protect ram spermatozoa against cold-shock. J Androl 27, 588 595.
    • (2005) J Androl , vol.27 , pp. 588-595
    • Barrios, B.1    Fernández-Juan, M.2    Muiño-Blanco, T.3    Cebrián-Pérez, J.A.4
  • 4
    • 21544475498 scopus 로고    scopus 로고
    • Isolation and characterization of the major proteins of ram seminal plasma
    • Bergeron A, Villemure M, Lazure C, Manjunath P, 2005 : Isolation and characterization of the major proteins of ram seminal plasma. Mol Reprod Dev 71, 461 470.
    • (2005) Mol Reprod Dev , vol.71 , pp. 461-470
    • Bergeron, A.1    Villemure, M.2    Lazure, C.3    Manjunath, P.4
  • 5
    • 0035122390 scopus 로고    scopus 로고
    • Isolation and identification of sperm membrane antigens recognized by antisperm antibodies, and their possible role in immunological infertility disease
    • Bohring C, Krause E, Habermann B, Krause W, 2001 : Isolation and identification of sperm membrane antigens recognized by antisperm antibodies, and their possible role in immunological infertility disease. Mol Human Reprod 7, 113 118.
    • (2001) Mol Human Reprod , vol.7 , pp. 113-118
    • Bohring, C.1    Krause, E.2    Habermann, B.3    Krause, W.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding
    • Bradford MM, 1976 : A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0033213244 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility
    • Brandon CI, Heusner GL, Caudle AB, Fayrer-Hosken RA, 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.L.2    Caudle, A.B.3    Fayrer-Hosken, R.A.4
  • 8
    • 0029026052 scopus 로고
    • Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: Effect of glycosylation on its heparin- and gelatin-binding capabilities
    • Calvete JJ, Mann K, Schäfer W, Sanz L, Reinert M, Nessau S, Raida M, Topfer-Petersen E, 1995 : Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities. Biochem J 310, 615 620.
    • (1995) Biochem J , vol.310 , pp. 615-620
    • Calvete, J.J.1    Mann, K.2    Schäfer, W.3    Sanz, L.4    Reinert, M.5    Nessau, S.6    Raida, M.7    Topfer-Petersen, E.8
  • 10
    • 0033163092 scopus 로고    scopus 로고
    • Attribute of fertile spermatozoa: An update
    • De Jonge C, 1999 : Attribute of fertile spermatozoa: an update. J Androl 20, 463 473.
    • (1999) J Androl , vol.20 , pp. 463-473
    • De Jonge, C.1
  • 11
    • 0028299296 scopus 로고
    • Characterization of the major proteins of bovine seminal fluid by two-dimensional polyacrylamide gel electrophoresis
    • Desnoyers L, Therien I, Manjunath P, 1994 : Characterization of the major proteins of bovine seminal fluid by two-dimensional polyacrylamide gel electrophoresis. Mol Reprod Dev 37, 425 435.
    • (1994) Mol Reprod Dev , vol.37 , pp. 425-435
    • Desnoyers, L.1    Therien, I.2    Manjunath, P.3
  • 12
    • 0019407604 scopus 로고
    • Proteins of human semen. I. Two-dimensional mapping of human seminal fluid
    • Edwards JJ, Tollaksen SL, Anderson NG, 1981 : Proteins of human semen. I. Two-dimensional mapping of human seminal fluid. Clin Chem 27, 1335 1340.
    • (1981) Clin Chem , vol.27 , pp. 1335-1340
    • Edwards, J.J.1    Tollaksen, S.L.2    Anderson, N.G.3
  • 13
    • 0020615925 scopus 로고
    • Primary structure of PDC-109, a major protein constituent of bovine seminal plasma
    • Esch FS, Ling NC, Bohlen P, Ying S, Guillemin R, 1983 : Primary structure of PDC-109, a major protein constituent of bovine seminal plasma. Biochem Biophys Res Commun 113, 861 867.
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 861-867
    • Esch, F.S.1    Ling, N.C.2    Bohlen, P.3    Ying, S.4    Guillemin, R.5
  • 15
    • 0030275817 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of bovine semen after cryopreservation in half-milliliter straws
    • Fraser GS, Bucci DM, Brooks CL, 1996 : Two-dimensional polyacrylamide gel electrophoresis of bovine semen after cryopreservation in half-milliliter straws. Theriogenology 46, 1103 1115.
    • (1996) Theriogenology , vol.46 , pp. 1103-1115
    • Fraser, G.S.1    Bucci, D.M.2    Brooks, C.L.3
  • 17
    • 0035992826 scopus 로고    scopus 로고
    • Prion protein is secreted in soluble forms in the epididymal fluid and proteolytically processed and transported in seminal plasma
    • Gatti JL, Metayer S, Moudjou M, Andreoletti O, Lantier F, Dacheux JL, Sarradin P, 2002 : Prion protein is secreted in soluble forms in the epididymal fluid and proteolytically processed and transported in seminal plasma. Biol Reprod 67, 393 400.
    • (2002) Biol Reprod , vol.67 , pp. 393-400
    • Gatti, J.L.1    Metayer, S.2    Moudjou, M.3    Andreoletti, O.4    Lantier, F.5    Dacheux, J.L.6    Sarradin, P.7
  • 18
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg A, Weiss W, Dunn MJ, 2004 : Current two-dimensional electrophoresis technology for proteomics. Proteomics 4, 3665 3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 19
    • 0035902554 scopus 로고    scopus 로고
    • Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes
    • Greube A, Müller K, Töpfer-Petersen E, Herrmann A, Müller P, 2001 : Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes. Biochemistry 40, 8326 8334.
    • (2001) Biochemistry , vol.40 , pp. 8326-8334
    • Greube, A.1    Müller, K.2    Töpfer-Petersen, E.3    Herrmann, A.4    Müller, P.5
  • 20
    • 0025057584 scopus 로고
    • Use of fluorescent probes to assess membrane integrity in mammalian spermatozoa
    • Harrison RAP, Vickers SE, 1990 : Use of fluorescent probes to assess membrane integrity in mammalian spermatozoa. J Reprod Fertil 88, 343 352.
    • (1990) J Reprod Fertil , vol.88 , pp. 343-352
    • Harrison, R.A.P.1    Vickers, S.E.2
  • 21
    • 0347657532 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability
    • Jobim MI, 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.1    Oberst, E.R.2    Salbego, C.G.3    Souza, D.O.4    Wald, V.B.5    Tramontina, F.6    Mattos, R.C.7
  • 23
    • 0023151638 scopus 로고
    • Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma
    • Manjunath P, Sairam MR, 1987 : Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma. Biochem J 241, 685 692.
    • (1987) Biochem J , vol.241 , pp. 685-692
    • Manjunath, P.1    Sairam, M.R.2
  • 24
  • 25
    • 0017889586 scopus 로고
    • Experimental approach to the study of semen and male reproductive function
    • Mann T, 1978 : Experimental approach to the study of semen and male reproductive function. Int J Fertil 23, 133 137.
    • (1978) Int J Fertil , vol.23 , pp. 133-137
    • Mann, T.1
  • 26
    • 30144443840 scopus 로고    scopus 로고
    • Peptide sequence analysis
    • Medzihradszky KF, 2005 : Peptide sequence analysis. Methods Enzymol 402, 209 244.
    • (2005) Methods Enzymol , vol.402 , pp. 209-244
    • Medzihradszky, K.F.1
  • 27
    • 0025284297 scopus 로고
    • Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin
    • Miller DJ, Winer MA, Ax RL, 1990 : Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin. Biol Reprod 42, 899 915.
    • (1990) Biol Reprod , vol.42 , pp. 899-915
    • Miller, D.J.1    Winer, M.A.2    Ax, R.L.3
  • 29
    • 33644604130 scopus 로고    scopus 로고
    • Identification of proteins in the accessory sex gland fluid associated with fertility indexes of dairy bulls: A proteomic approach
    • Moura AA, Koc H, Chapman DA, Killian GJ, 2006 : Identification of proteins in the accessory sex gland fluid associated with fertility indexes of dairy bulls: a proteomic approach. J Androl 27, 201 211.
    • (2006) J Androl , vol.27 , pp. 201-211
    • Moura, A.A.1    Koc, H.2    Chapman, D.A.3    Killian, G.J.4
  • 30
    • 0017696571 scopus 로고
    • High resolution of two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrel PZ, Goodman HM, O'Farrel 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'Farrel, P.Z.1    Goodman, H.M.2    O'Farrel, P.H.3
  • 31
    • 0030473039 scopus 로고    scopus 로고
    • Viability of ram spermatozoa in relation to the abstinence period and successive ejaculations
    • Ollero M, Muiño-Blanco T, López-Pérez M, Cebrián-Pérez JA, 1996 : Viability of ram spermatozoa in relation to the abstinence period and successive ejaculations. Int J Androl 19, 287 292.
    • (1996) Int J Androl , vol.19 , pp. 287-292
    • Ollero, M.1    Muiño-Blanco, T.2    López-Pérez, M.3    Cebrián-Pérez, J.A.4
  • 32
    • 0030198410 scopus 로고    scopus 로고
    • Evidence that frozen/thawed ram spermatozoa show accelerated capacitation in vitro as assessed by chlortetracycline assay
    • Perez LJ, Valcarcel A, Delasheras MA, Moses D, Baldassarre H, 1996 : Evidence that frozen/thawed ram spermatozoa show accelerated capacitation in vitro as assessed by chlortetracycline assay. Theriogenology 46, 131 140.
    • (1996) Theriogenology , vol.46 , pp. 131-140
    • Perez, L.J.1    Valcarcel, A.2    Delasheras, M.A.3    Moses, D.4    Baldassarre, H.5
  • 33
    • 0035949201 scopus 로고    scopus 로고
    • Seasonal differences in ram seminal plasma revealed by partition in an aqueous two-phase system
    • Pérez-Pé R, Barrios B, Muiño-Blanco T, Cebrián-Pérez JA, 2001a : Seasonal differences in ram seminal plasma revealed by partition in an aqueous two-phase system. J Chrom B 760, 113 121.
    • (2001) J Chrom B , vol.760 , pp. 113-121
    • Pérez-Pé, R.1    Barrios, B.2    Muiño-Blanco, T.3    Cebrián-Pérez, J.A.4
  • 34
    • 0035424482 scopus 로고    scopus 로고
    • Semen plasma proteins prevent cold-shock membrane damage to ram spermatozoa
    • Pérez-Pé R, Cebrián-Pérez JA, Muiño-Blanco T, 2001b : Semen plasma proteins prevent cold-shock membrane damage to ram spermatozoa. Theriogenology 56, 425 434.
    • (2001) Theriogenology , vol.56 , pp. 425-434
    • Pérez-Pé, R.1    Cebrián-Pérez, J.A.2    Muiño-Blanco, T.3
  • 35
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS, 1999 : Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551 3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 36
    • 0029937184 scopus 로고    scopus 로고
    • Solubilization of proteins for electrophoretic analyses
    • Rabilloud T, 1996 : Solubilization of proteins for electrophoretic analyses. Electrophoresis 17, 813 829.
    • (1996) Electrophoresis , vol.17 , pp. 813-829
    • Rabilloud, T.1
  • 37
    • 0027263129 scopus 로고
    • Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: A dual role for spermadhesins in fertilization
    • Sanz L, Calvete JJ, Mann K, Gabius HJ, Topfer-Petersen E, 1993 : Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: a dual role for spermadhesins in fertilization. Mol Reprod Dev 35, 37 43.
    • (1993) Mol Reprod Dev , vol.35 , pp. 37-43
    • Sanz, L.1    Calvete, J.J.2    Mann, K.3    Gabius, H.J.4    Topfer-Petersen, E.5
  • 39
    • 0022337980 scopus 로고
    • Deglycosylation of alpha 1-proteinase inhibitor by endo-beta-N- acetylglucosaminidase F
    • Steube K, Gross V, Heinrich PC, 1985 : Deglycosylation of alpha 1-proteinase inhibitor by endo-beta-N-acetylglucosaminidase F. Biochemistry 24, 5587 5592.
    • (1985) Biochemistry , vol.24 , pp. 5587-5592
    • Steube, K.1    Gross, V.2    Heinrich, P.C.3
  • 40
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F
    • Tarentino AL, Gomez CM, Plummer TH Jr., 1985 : Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F. Biochemistry 24, 4665 4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 41
    • 4344653751 scopus 로고    scopus 로고
    • Isolation and characterization of gelatin-binding proteins from goat seminal plasma
    • Villemure M, Lazure C, Manjunath P, 2003 : Isolation and characterization of gelatin-binding proteins from goat seminal plasma. Reprod Biol Endocrinol 1, 39.
    • (2003) Reprod Biol Endocrinol , vol.1 , pp. 39
    • Villemure, M.1    Lazure, C.2    Manjunath, P.3
  • 42
    • 0029461068 scopus 로고
    • Recent developments and concepts in the cryopreservation of spermatozoa and the assessment of their post-thawing function
    • Watson PF, 1995 : Recent developments and concepts in the cryopreservation of spermatozoa and the assessment of their post-thawing function. Reprod Fertil Dev 7, 871 891.
    • (1995) Reprod Fertil Dev , vol.7 , pp. 871-891
    • Watson, P.F.1
  • 43
    • 0003931045 scopus 로고
    • In: Knobil, E., Neil, J.D. (. ed. Raven Press, New York. The Physiology of Reproduction.
    • Yanagimachi R, 1994 : Mammalian fertilization. In : Knobil E, Neil JD (ed Raven Press, New York. The Physiology of Reproduction.
    • (1994) Mammalian Fertilization
    • Yanagimachi, R.1


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