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Volumn 51, Issue 4, 1998, Pages 362-372

GPx3: The plasma-type glutathione peroxidase is expressed under androgenic control in the mouse epididymis and vas deferens

Author keywords

Caput corpus cauda epididymidis; Hydrogen peroxyde; Oxydative stress; Polyclonal antibody; Sperm maturation

Indexed keywords

GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; MESSENGER RNA; POLYCLONAL ANTIBODY;

EID: 0031791849     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2795(199812)51:4<362::AID-MRD2>3.0.CO;2-L     Document Type: Article
Times cited : (50)

References (57)
  • 1
    • 0029919631 scopus 로고    scopus 로고
    • The extragenomic action of progesterone on human spermatozoa is influenced by redox regulated changes in tyrosine phosphorylation during capacitation
    • Aitken RJ, Buckingam DW, Harkiss D, Paterson M, Fisher H, Irvine DS (1996): The extragenomic action of progesterone on human spermatozoa is influenced by redox regulated changes in tyrosine phosphorylation during capacitation. Mol Cell Endocrinol 117:83-93.
    • (1996) Mol Cell Endocrinol , vol.117 , pp. 83-93
    • Aitken, R.J.1    Buckingam, D.W.2    Harkiss, D.3    Paterson, M.4    Fisher, H.5    Irvine, D.S.6
  • 2
    • 0023617012 scopus 로고
    • Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa
    • Aitken RJ, Clarkson JS (1987): Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa. J Reprod Fertil 81:459-469.
    • (1987) J Reprod Fertil , vol.81 , pp. 459-469
    • Aitken, R.J.1    Clarkson, J.S.2
  • 3
    • 0024427034 scopus 로고
    • Generation of reactive oxygen species, lipid peroxidation, and human sperm function
    • Aitken RJ, Clarkson JS, Fishel S (1989): Generation of reactive oxygen species, lipid peroxidation, and human sperm function. Biol Reprod 40:183-197.
    • (1989) Biol Reprod , vol.40 , pp. 183-197
    • Aitken, R.J.1    Clarkson, J.S.2    Fishel, S.3
  • 4
    • 0029046131 scopus 로고
    • Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function
    • Aitken RJ, Paterson M, Fisher H (1995): Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function. J Cell Sci 180:2017-2025.
    • (1995) J Cell Sci , vol.180 , pp. 2017-2025
    • Aitken, R.J.1    Paterson, M.2    Fisher, H.3
  • 5
    • 0023412036 scopus 로고
    • Spontaneous lipid peroxidation and production of hydrogen peroxide and Superoxide in human spermatozoa: Superoxide dismutase as a major enzyme protectant against oxygen toxicity
    • Alvarez JG, Touchtone JC, Blasco L, Storey B.T (1987): Spontaneous lipid peroxidation and production of hydrogen peroxide and Superoxide in human spermatozoa: Superoxide dismutase as a major enzyme protectant against oxygen toxicity. J Androl 8:338-348.
    • (1987) J Androl , vol.8 , pp. 338-348
    • Alvarez, J.G.1    Touchtone, J.C.2    Blasco, L.3    Storey, B.T.4
  • 6
    • 0021138997 scopus 로고
    • Lipid peroxidation and the reactions of Superoxide and hydrogen peroxide in mouse spermatozoa
    • Alvarez JG, Storey B.T (1984): Lipid peroxidation and the reactions of Superoxide and hydrogen peroxide in mouse spermatozoa. Biol Reprod 30:833-841.
    • (1984) Biol Reprod , vol.30 , pp. 833-841
    • Alvarez, J.G.1    Storey, B.T.2
  • 8
    • 0026032205 scopus 로고
    • Hydrogen peroxide is involved in hamster sperm capacitation in vitro
    • Bize I, Santander G, Cabello P, Driscoll D, Sharpe C (1991): Hydrogen peroxide is involved in hamster sperm capacitation in vitro. Biol Reprod 44:398-403.
    • (1991) Biol Reprod , vol.44 , pp. 398-403
    • Bize, I.1    Santander, G.2    Cabello, P.3    Driscoll, D.4    Sharpe, C.5
  • 9
    • 0026773732 scopus 로고
    • Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, breast in humans and rodents
    • Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF (1992): Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, breast in humans and rodents. Blood 79:3233-3238.
    • (1992) Blood , vol.79 , pp. 3233-3238
    • Chu, F.F.1    Esworthy, R.S.2    Doroshow, J.H.3    Doan, K.4    Liu, X.F.5
  • 10
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue-distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu FF, Doroshow JH, Esworthy RS (1993): Expression, characterization, and tissue-distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem 268:2571-2576.
    • (1993) J Biol Chem , vol.268 , pp. 2571-2576
    • Chu, F.F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 11
    • 0026688587 scopus 로고
    • Reactive oxygen species and human spermatozoa
    • de Lamirande E, Gagnon C (1992): Reactive oxygen species and human spermatozoa. J Androl 13:368-378.
    • (1992) J Androl , vol.13 , pp. 368-378
    • De Lamirande, E.1    Gagnon, C.2
  • 12
    • 0027426055 scopus 로고
    • Inverse relationship between the induction of human sperm capacitation and spontaneous acrosome reaction by various biological fluids and the Superoxide scavenging capacity of these fluids
    • de Lamirande E, Eiley D, Gagnon C (1993): Inverse relationship between the induction of human sperm capacitation and spontaneous acrosome reaction by various biological fluids and the Superoxide scavenging capacity of these fluids. Int J Androl 16:258-266.
    • (1993) Int J Androl , vol.16 , pp. 258-266
    • De Lamirande, E.1    Eiley, D.2    Gagnon, C.3
  • 13
    • 0031091039 scopus 로고    scopus 로고
    • Capacitation as a regulatory event that primes spermatozoa for the acrosome reaction and fertilization
    • de Lamirande E, Leclerc P, Gagnon C (1997): Capacitation as a regulatory event that primes spermatozoa for the acrosome reaction and fertilization. Mol Hum Reprod 3:175-194.
    • (1997) Mol Hum Reprod , vol.3 , pp. 175-194
    • De Lamirande, E.1    Leclerc, P.2    Gagnon, C.3
  • 14
    • 0028244191 scopus 로고
    • GATA-type zinc finger motif containing sequences and choriongene transcription factors of the silkworm Bombyx mori
    • Drevet JR, Skeiky YAW, Iatrou K (1994): GATA-type zinc finger motif containing sequences and choriongene transcription factors of the silkworm Bombyx mori. J Biol Chem 269:10660-10667.
    • (1994) J Biol Chem , vol.269 , pp. 10660-10667
    • Drevet, J.R.1    Skeiky, Y.A.W.2    Iatrou, K.3
  • 15
    • 0029829262 scopus 로고    scopus 로고
    • Structural organization, chromosomal localization, expression, and phylogenetic evaluation of mouse glutathione peroxidase encoding genes
    • Dufaure J-P, Lareyre J-J, Schwaab V, Mattei M-G, Drevet JR (1996): Structural organization, chromosomal localization, expression, and phylogenetic evaluation of mouse glutathione peroxidase encoding genes. CR Acad Sci III 319:559-568.
    • (1996) CR Acad Sci III , vol.319 , pp. 559-568
    • Dufaure, J.-P.1    Lareyre, J.-J.2    Schwaab, V.3    Mattei, M.-G.4    Drevet, J.R.5
  • 16
    • 0025754084 scopus 로고
    • Characterization and partial amino acid sequence of human plasma glutathione peroxidase
    • Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow H (1991): Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys 286:330-336.
    • (1991) Arch Biochem Biophys , vol.286 , pp. 330-336
    • Esworthy, R.S.1    Chu, F.F.2    Paxton, R.J.3    Akman, S.4    Doroshow, H.5
  • 17
    • 0026099693 scopus 로고
    • Specific distribution of messenger ribonucleic acids for 24-kilodalton proteins in the mouse epididymis as revealed by in situ hybridization: Developmental expression and regulation in adults
    • Faure J, Ghyselnck N, Jimenez C, Dufaure J-P (1991): Specific distribution of messenger ribonucleic acids for 24-kilodalton proteins in the mouse epididymis as revealed by in situ hybridization: Developmental expression and regulation in adults. Biol Reprod 44:13-22.
    • (1991) Biol Reprod , vol.44 , pp. 13-22
    • Faure, J.1    Ghyselnck, N.2    Jimenez, C.3    Dufaure, J.-P.4
  • 18
    • 0031127073 scopus 로고    scopus 로고
    • Comparative analysis of the ability of precursor germ cells and epididymal spermatozoa to generate reactive oxygen metabolites
    • Fisher HM and Aitken RJ (1997): Comparative analysis of the ability of precursor germ cells and epididymal spermatozoa to generate reactive oxygen metabolites. J Exp Zool 277:390-400.
    • (1997) J Exp Zool , vol.277 , pp. 390-400
    • Fisher, H.M.1    Aitken, R.J.2
  • 19
    • 0001412723 scopus 로고
    • Glutathione peroxidase brought into focus
    • WA Pryor (ed): New York: Academic Press
    • Flohé L (1982): Glutathione peroxidase brought into focus. In WA Pryor (ed): "Free Radicals in Biology." New York: Academic Press, pp 223-253.
    • (1982) Free Radicals in Biology , pp. 223-253
    • Flohé, L.1
  • 20
    • 3643102317 scopus 로고
    • Detrimental and beneficial effects of reactive oxygen species on sperm function
    • Gagnon C, de Lamirande E (1994): Detrimental and beneficial effects of reactive oxygen species on sperm function. Perspect Assist Reprod 4:121-127.
    • (1994) Perspect Assist Reprod , vol.4 , pp. 121-127
    • Gagnon, C.1    De Lamirande, E.2
  • 21
    • 0026341516 scopus 로고
    • Sequence homology of androgen-regulated epididymal proteins with glutathione peroxidase in mice
    • Ghyselinck N, Jimenez C, Dufaure J-P (1991): Sequence homology of androgen-regulated epididymal proteins with glutathione peroxidase in mice. J Reprod Fertil 93:461-166.
    • (1991) J Reprod Fertil , vol.93 , pp. 461-1166
    • Ghyselinck, N.1    Jimenez, C.2    Dufaure, J.-P.3
  • 22
    • 0027518840 scopus 로고
    • Structural organization and regulation of the gene for the androgen-dependent glutathione peroxidase-like protein specific to the mouse epididymis
    • Ghyselinck N, Dufaure I, Lareyre J-J, Rigaudière N, Mattei M-G, Dufaure J-P (1993): Structural organization and regulation of the gene for the androgen-dependent glutathione peroxidase-like protein specific to the mouse epididymis. Mol Endocrinol 7:258-272.
    • (1993) Mol Endocrinol , vol.7 , pp. 258-272
    • Ghyselinck, N.1    Dufaure, I.2    Lareyre, J.-J.3    Rigaudière, N.4    Mattei, M.-G.5    Dufaure, J.-P.6
  • 23
    • 0029432515 scopus 로고
    • Oxidative stress and living cells
    • Gille G, Sigler K (1995): Oxidative stress and living cells. Folia Microbiol 40:131-152.
    • (1995) Folia Microbiol , vol.40 , pp. 131-152
    • Gille, G.1    Sigler, K.2
  • 24
    • 0028670194 scopus 로고
    • An in vitro promoting role for hydrogen peroxide in human sperm capacitation
    • Griveau J.F, Renard P, Le Lannou D (1994): An in vitro promoting role for hydrogen peroxide in human sperm capacitation. Int J Androl 17:300-307.
    • (1994) Int J Androl , vol.17 , pp. 300-307
    • Griveau, J.F.1    Renard, P.2    Le Lannou, D.3
  • 25
  • 27
    • 0026540891 scopus 로고
    • Formation of reactive oxygen species in spermatozoa of fertile patients
    • Iwasaki A, Gagnon C (1992): Formation of reactive oxygen species in spermatozoa of fertile patients. Fertil Steril 57:409-416.
    • (1992) Fertil Steril , vol.57 , pp. 409-416
    • Iwasaki, A.1    Gagnon, C.2
  • 28
    • 0025342020 scopus 로고
    • Immunochemical localization and association with spermatozoa of androgenregulated protein of MR 24000 secreted by the mouse epididymis
    • Jimenez C, Ghyselinck N, Depeiges A, Dufaure J-P (1990): Immunochemical localization and association with spermatozoa of androgenregulated protein of MR 24000 secreted by the mouse epididymis. Biol Cell 68:171-174.
    • (1990) Biol Cell , vol.68 , pp. 171-174
    • Jimenez, C.1    Ghyselinck, N.2    Depeiges, A.3    Dufaure, J.-P.4
  • 29
    • 0018341406 scopus 로고
    • Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acids peroxides, and protective action of seminal plasma
    • Jones R, Mann T. Sherins R (1979): Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acids peroxides, and protective action of seminal plasma. Fertil Steril 31:531-537.
    • (1979) Fertil Steril , vol.31 , pp. 531-537
    • Jones, R.1    Mann, T.2    Sherins, R.3
  • 30
    • 0030965988 scopus 로고    scopus 로고
    • Characterization of an androgen response element within the promoter of the epididymis-specific murine glutathione peroxidase 5 gene
    • Lareyre J-J, Claessens F, Rombauts W, Dufaure J-P, Drevet JR (1997): Characterization of an androgen response element within the promoter of the epididymis-specific murine glutathione peroxidase 5 gene. Mol Cell Endocrinol 129:33-46.
    • (1997) Mol Cell Endocrinol , vol.129 , pp. 33-46
    • Lareyre, J.-J.1    Claessens, F.2    Rombauts, W.3    Dufaure, J.-P.4    Drevet, J.R.5
  • 31
    • 0023522192 scopus 로고
    • Characterization of the major hydroperoxide reducing activity of human plasma: Purification and properties of a selenium dependent glutathione peroxidase
    • Maddipati KR, Marnett LJ (1987): Characterization of the major hydroperoxide reducing activity of human plasma: Purification and properties of a selenium dependent glutathione peroxidase. J Biol Chem 262:17398-17403.
    • (1987) J Biol Chem , vol.262 , pp. 17398-17403
    • Maddipati, K.R.1    Marnett, L.J.2
  • 33
    • 0027320750 scopus 로고
    • Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular ciliary epithelium: Expression of the plasma and cellular forms within the mammalian eye
    • Martin-Alonso JM, Ghosh S, Coca-Prados M (1993): Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular ciliary epithelium: Expression of the plasma and cellular forms within the mammalian eye. J Biochem 114:284-291.
    • (1993) J Biochem , vol.114 , pp. 284-291
    • Martin-Alonso, J.M.1    Ghosh, S.2    Coca-Prados, M.3
  • 34
    • 0027993038 scopus 로고
    • Mouse plasma glutathione peroxidase: cDNA sequence analysis and renal proximal tubular expression and secretion
    • Maser RL, Magenheimer BS, Calvet JP (1994): Mouse plasma glutathione peroxidase: cDNA sequence analysis and renal proximal tubular expression and secretion. J Biol Chem 269:27066-27073.
    • (1994) J Biol Chem , vol.269 , pp. 27066-27073
    • Maser, R.L.1    Magenheimer, B.S.2    Calvet, J.P.3
  • 35
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • Mills GC (1957): Hemoglobin catabolism. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem 229:189-197.
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 36
    • 0021942998 scopus 로고
    • Regional differences in luminal fluid of the rat testis and epididymis revealed by two-dimensional gel electrophoresis
    • Olson GE and Hinton BT (1985): Regional differences in luminal fluid of the rat testis and epididymis revealed by two-dimensional gel electrophoresis. J Androl 6:20-34.
    • (1985) J Androl , vol.6 , pp. 20-34
    • Olson, G.E.1    Hinton, B.T.2
  • 37
    • 0026714544 scopus 로고
    • Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon
    • Perry A, Jones R, Niang LSP, Jakson RM, Hall L (1992): Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon. Biochem J 285:863-870.
    • (1992) Biochem J , vol.285 , pp. 863-870
    • Perry, A.1    Jones, R.2    Niang, L.S.P.3    Jakson, R.M.4    Hall, L.5
  • 38
    • 0027979010 scopus 로고
    • Reactive oxygen species released by activated neutrophils, but not by deficient spermatozoa, are sufficient to affect normal sperm motility
    • Plante M, de Lamirande E, Gagnon C (1994): Reactive oxygen species released by activated neutrophils, but not by deficient spermatozoa, are sufficient to affect normal sperm motility. Fertil Steril 62:387-393.
    • (1994) Fertil Steril , vol.62 , pp. 387-393
    • Plante, M.1    De Lamirande, E.2    Gagnon, C.3
  • 39
    • 0027468676 scopus 로고
    • Testosterone regulates mitochondrial aspartate aminotransferase gene expression and mRNA stability in prostate
    • Quian K, Franklin RB, Costello LC (1993): Testosterone regulates mitochondrial aspartate aminotransferase gene expression and mRNA stability in prostate. J Steroid Biochem 44:13-19.
    • (1993) J Steroid Biochem , vol.44 , pp. 13-19
    • Quian, K.1    Franklin, R.B.2    Costello, L.C.3
  • 42
    • 0029617643 scopus 로고
    • Cloning of the mouse gene encoding plasma glutathione peroxidase: Organization, sequence, and chromosomal localization
    • Schwaab V, Baud E, Ghyselinck N, Mattéi M-G, Dufaure J-P, Drevet JR (1995): Cloning of the mouse gene encoding plasma glutathione peroxidase: Organization, sequence, and chromosomal localization. Gene 167:25-31.
    • (1995) Gene , vol.167 , pp. 25-31
    • Schwaab, V.1    Baud, E.2    Ghyselinck, N.3    Mattéi, M.-G.4    Dufaure, J.-P.5    Drevet, J.R.6
  • 43
    • 0031090459 scopus 로고    scopus 로고
    • Biochemistry of the induction and prevention of lipoperoxidative damage in human spermatozoa
    • Storey BT (1997): Biochemistry of the induction and prevention of lipoperoxidative damage in human spermatozoa. Mol Hum Reprod 3:203-213.
    • (1997) Mol Hum Reprod , vol.3 , pp. 203-213
    • Storey, B.T.1
  • 44
    • 0019193368 scopus 로고
    • Structure, synthesis, and function of glutathione peroxidase
    • Sunde RA and Hoekstra WG (1980): Structure, synthesis, and function of glutathione peroxidase. Nutr Rev 38:265-273.
    • (1980) Nutr Rev , vol.38 , pp. 265-273
    • Sunde, R.A.1    Hoekstra, W.G.2
  • 45
    • 0022471869 scopus 로고
    • Selenium-dependent glutathione peroxidase protein and activity: Immunological investigations on cellular and plasma enzymes
    • Takahashi K, Cohen H (1986): Selenium-dependent glutathione peroxidase protein and activity: Immunological investigations on cellular and plasma enzymes. Blood 68:640-645.
    • (1986) Blood , vol.68 , pp. 640-645
    • Takahashi, K.1    Cohen, H.2
  • 46
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme
    • Takahashi K, Avissar N, Whithin J, Cohen H (1987): Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme. Arch Biochem Biophys 256:677-686.
    • (1987) Arch Biochem Biophys , vol.256 , pp. 677-686
    • Takahashi, K.1    Avissar, N.2    Whithin, J.3    Cohen, H.4
  • 48
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F, Maiorino M, Gregolin C (1985): The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochem Biophys Acta 839:62-70.
    • (1985) Biochem Biophys Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 49
    • 0026475609 scopus 로고
    • An effect of androgens on the length of the poly(A)-tail and alternative splicing cause size heterogeneity of the messenger ribonucleic acids encoding cystatin-related protein
    • Vercaeren I, Winderickx J, Devos A, Peeters B, Heyns W (1992): An effect of androgens on the length of the poly(A)-tail and alternative splicing cause size heterogeneity of the messenger ribonucleic acids encoding cystatin-related protein. Endocrinology 131:2496-2502.
    • (1992) Endocrinology , vol.131 , pp. 2496-2502
    • Vercaeren, I.1    Winderickx, J.2    Devos, A.3    Peeters, B.4    Heyns, W.5
  • 50
    • 0030348185 scopus 로고    scopus 로고
    • In vitro expresion of a mouse tissue-specific glutathione peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against peroxidative damage
    • Vernet P, Rigaudière N, Ghyselinck N, Dufaure J-P, Drevet JR (1996): In vitro expresion of a mouse tissue-specific glutathione peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against peroxidative damage. Biochem Cell Biol 74:125-131.
    • (1996) Biochem Cell Biol , vol.74 , pp. 125-131
    • Vernet, P.1    Rigaudière, N.2    Ghyselinck, N.3    Dufaure, J.-P.4    Drevet, J.R.5
  • 51
    • 0030902169 scopus 로고    scopus 로고
    • Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPx5, a murine epididymis-specific glutathione peroxidase
    • Vernet P, Faure J, Dufaure J-P, Drevet JR (1997): Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPx5, a murine epididymis-specific glutathione peroxidase. Mol Reprod Dev 47:87-98.
    • (1997) Mol Reprod Dev , vol.47 , pp. 87-98
    • Vernet, P.1    Faure, J.2    Dufaure, J.-P.3    Drevet, J.R.4
  • 52
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa: Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS (1995): Capacitation of mouse spermatozoa: Correlation between the capacitation state and protein tyrosine phosphorylation. Development 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 53
    • 0024359610 scopus 로고
    • Relationship between calcium, AMP, ATP, intracellular pH, and the capacity of hamster spermatozoa to express hyperactivated motility
    • White DR, Aitken RJ (1989): Relationship between calcium, AMP, ATP, intracellular pH, and the capacity of hamster spermatozoa to express hyperactivated motility. Gamete Res 22:163-178.
    • (1989) Gamete Res , vol.22 , pp. 163-178
    • White, D.R.1    Aitken, R.J.2
  • 55
    • 0025309247 scopus 로고
    • An improved conjugation method for controlled covalent coupling of synthetic peptides to proteins using glutaraldehyde in a dialysis method
    • Zegers N, Gerritse J, Deen C, Boersma W, Claassen E (1990): An improved conjugation method for controlled covalent coupling of synthetic peptides to proteins using glutaraldehyde in a dialysis method. J Immunol Meth 130:195-200.
    • (1990) J Immunol Meth , vol.130 , pp. 195-200
    • Zegers, N.1    Gerritse, J.2    Deen, C.3    Boersma, W.4    Claassen, E.5
  • 56
    • 0027324127 scopus 로고
    • Reactive oxygen species in semen of infertile patients: Levels of Superoxide dismutase-and catalase-like activities in seminal plasma and spermatozoa
    • Zini A, de Lamirande E, Gagnon C (1993): Reactive oxygen species in semen of infertile patients: Levels of Superoxide dismutase-and catalase-like activities in seminal plasma and spermatozoa. Int J Androl 16:183-188.
    • (1993) Int J Androl , vol.16 , pp. 183-188
    • Zini, A.1    De Lamirande, E.2    Gagnon, C.3
  • 57
    • 0030880086 scopus 로고    scopus 로고
    • Identification and characterization of antioxidant enzyme mRNAs in the rat epididymis
    • Zini A, Schlegel PN (1997): Identification and characterization of antioxidant enzyme mRNAs in the rat epididymis. Int J Androl 20:86-91.
    • (1997) Int J Androl , vol.20 , pp. 86-91
    • Zini, A.1    Schlegel, P.N.2


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