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Volumn 68, Issue , 2002, Pages 694-699

Vitellogenesis in Aquatic Animals

Author keywords

endocrine disrupters; fish; lipovitellin; phosvitin; proteolysis; vitellogenin; component

Indexed keywords


EID: 0037770181     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.2331/fishsci.68.sup1_694     Document Type: Article
Times cited : (83)

References (56)
  • 1
    • 0000526993 scopus 로고
    • Vitellogenic blood protein synthesis by insect fat body
    • Pan, M. J., Bell, W. J. and Telfer, W. H. Vitellogenic blood protein synthesis by insect fat body. Science 1969; 165: 393–394.
    • (1969) Science , vol.165 , pp. 393-394
    • Pan, M.J.1    Bell, W.J.2    Telfer, W.H.3
  • 2
    • 0022163146 scopus 로고
    • Vitellogenesis and oocyte growth in non-mammalian vertebrates
    • In: Browder L. W., editor 1. NY: Plenum Press
    • Wallace, R. A. Vitellogenesis and oocyte growth in non-mammalian vertebrates. In: Browder L. W., editor. Develop-mental Biology 1. NY: Plenum Press. 1985: p 127–177.
    • (1985) Develop-mental Biology , pp. 127-177
    • Wallace, R.A.1
  • 3
    • 77956833641 scopus 로고
    • Vitellogenesis and oocyte assembly
    • In Hoar W. S., Randall D. J. (eds.) New York: Academic Press
    • Mommsen, T. P. and Walsh, P. L. Vitellogenesis and oocyte assembly. In: Hoar W. S., Randall D. J. (eds.), Fish Physiology XI. New York: Academic Press; 1988: 347–406.
    • (1988) Fish Physiology , vol.11 , pp. 347-406
    • Mommsen, T.P.1    Walsh, P.L.2
  • 4
    • 0002090118 scopus 로고
    • Vitellogenesis in fishes: status and perspectives
    • In: Davey K. G., Peter R. E., Tobe S. S. (eds.,) Ottawa: National Research Council
    • Specker, J. L. and Sullivan, C. V. Vitellogenesis in fishes: status and perspectives. In: Davey K. G., Peter R. E., Tobe S. S. (eds.,), Perspectives in Comparative Endocrinology. Ottawa: National Research Council; 1994: 304–315.
    • (1994) Perspectives in Comparative Endocrinology. , pp. 304-315
    • Specker, J.L.1    Sullivan, C.V.2
  • 5
    • 0018408072 scopus 로고
    • Vitellogenin in Xenopus laevis is encoded in a small family of genes
    • Wahli, W., Dawid, I. B., Wyler, T., Jaggi, R. B., Weber, R. and Ryffel, G. U. Vitellogenin in Xenopus laevis is encoded in a small family of genes. Cell. 1979; 16(3): 535–549.
    • (1979) Cell. , vol.16 , Issue.3 , pp. 535-549
    • Wahli, W.1    Dawid, I.B.2    Wyler, T.3    Jaggi, R.B.4    Weber, R.5    Ryffel, G.U.6
  • 6
    • 0018825490 scopus 로고
    • Isolation and translation in vitro of four related vitellogenin mRNAs of estrogen-stimulated Xenopus laevis
    • Felber, B. K., Maurhofer, S., Jaggi, R. B., Wyler, T., Wahli, W., Ryffel, G. U. and Weber, R. Isolation and translation in vitro of four related vitellogenin mRNAs of estrogen-stimulated Xenopus laevis. Eur. J. Biochem. 1980; 105(1): 17–24.
    • (1980) Eur. J. Biochem. , vol.105 , Issue.1 , pp. 17-24
    • Felber, B.K.1    Maurhofer, S.2    Jaggi, R.B.3    Wyler, T.4    Wahli, W.5    Ryffel, G.U.6    Weber, R.7
  • 7
    • 0023660763 scopus 로고
    • Nucleotide sequences of a chicken vitellogenin gene and derived amino acid sequence of the enclosed yolk precursor proteia
    • van-het Schip, F. D., Samallo, J., Broos, J., Ophuis, J., Mojet, M., Gruber, M. and AB, G. Nucleotide sequences of a chicken vitellogenin gene and derived amino acid sequence of the enclosed yolk precursor proteia J. Mol. Biol. 1987; 196: 245–300.
    • (1987) J. Mol. Biol. , vol.196 , pp. 245-300
    • van-het Schip, F.D.1    Samallo, J.2    Broos, J.3    Ophuis, J.4    Mojet, M.5    Gruber, M.6    AB, G.7
  • 8
    • 0024345781 scopus 로고
    • The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other
    • Silva, R., Fischer, A. H. and Burch, J. B. The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other Mol. Cell Biol. 1989; 9(8): 3557–3562.
    • (1989) Mol. Cell Biol. , vol.9 , Issue.8 , pp. 3557-3562
    • Silva, R.1    Fischer, A.H.2    Burch, J.B.3
  • 9
    • 0029123767 scopus 로고
    • Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein
    • LaFleur, G. J. Jr, Byrne, B. M., Kanungo, J., Nelson, L D., Greenberg, R. M. and Wallace, R. A. Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein. J. Mol. Evol. 1995; 41: 505–521.
    • (1995) J. Mol. Evol. , vol.41 , pp. 505-521
    • LaFleur, G.J.1    Byrne, B.M.2    Kanungo, J.3    Nelson, L.D.4    Greenberg, R.M.5    Wallace, R.A.6
  • 11
    • 0028018471 scopus 로고
    • Two major groups of vitellogenin cDNA clones from Oreochromis aureus (Steindachner)
    • Lee, B. H., Lim, E. H., Lam, T. J. and Ding, J. L. Two major groups of vitellogenin cDNA clones from Oreochromis aureus (Steindachner). Biochem. Mol.Biol Int. 1994; 34:75–83.
    • (1994) Biochem. Mol.Biol Int. , vol.34 , pp. 75-83
    • Lee, B.H.1    Lim, E.H.2    Lam, T.J.3    Ding, J.L.4
  • 12
    • 0034525388 scopus 로고    scopus 로고
    • Estrogen-induced vitellogenin mRNA and protein in sheepshead minnow (Cyprinodon variegatus)
    • Bowman, C. J., Kroll, K. J., Hemmer, M. J., Folmer, L. C. and Denslow, N. D. Estrogen-induced vitellogenin mRNA and protein in sheepshead minnow (Cyprinodon variegatus). Gen. Comp. Endocrinol. 2000; 120: 300–313.
    • (2000) Gen. Comp. Endocrinol. , vol.120 , pp. 300-313
    • Bowman, C.J.1    Kroll, K.J.2    Hemmer, M.J.3    Folmer, L.C.4    Denslow, N.D.5
  • 13
    • 0030603225 scopus 로고    scopus 로고
    • Characterization of vitellogenin from rainbow trout (Oncorhynchus mykiss)
    • Mouchel, N., Trichet, V., Betz, A., Le Pennec, J. P. and Wolff, J. Characterization of vitellogenin from rainbow trout (Oncorhynchus mykiss). Gene 1996; 174: 59–64.
    • (1996) Gene , vol.174 , pp. 59-64
    • Mouchel, N.1    Trichet, V.2    Betz, A.3    Le Pennec, J.P.4    Wolff, J.5
  • 15
    • 0033835317 scopus 로고    scopus 로고
    • Genomic analysis of the vitellogenin locus in rainbow trout (Oncorhynchus mykiss) reveals a complex history of gene amplification and retroposon activity
    • Trichet, V., Buisine, N., Mouchel, N., Moran, P., Pendas, A. M., Le Pennec, J. P. and Wolff, J. Genomic analysis of the vitellogenin locus in rainbow trout (Oncorhynchus mykiss) reveals a complex history of gene amplification and retroposon activity. Mol. Gen. Genet. 2000; 263(5): 828–837.
    • (2000) Mol. Gen. Genet. , vol.263 , Issue.5 , pp. 828-837
    • Trichet, V.1    Buisine, N.2    Mouchel, N.3    Moran, P.4    Pendas, A.M.5    Le Pennec, J.P.6    Wolff, J.7
  • 16
    • 0034601707 scopus 로고    scopus 로고
    • A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene
    • Wang, H., Yan, T., Tan, J. T. T. and Gong, Z. A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene. Gene. 2000; 256: 303–310.
    • (2000) Gene. , vol.256 , pp. 303-310
    • Wang, H.1    Yan, T.2    Tan, J.T.T.3    Gong, Z.4
  • 17
    • 0034743640 scopus 로고    scopus 로고
    • Effects of estradiol-17β treatment on in vitro and in vivo synthesis of two distinct vitellogenins in tilapia
    • Takemura, A. and Kim, B. H. Effects of estradiol-17β treatment on in vitro and in vivo synthesis of two distinct vitellogenins in tilapia. Comp. Biochem. Physiol. 2001; 129(A): 641–651.
    • (2001) Comp. Biochem. Physiol. , vol.129 , Issue.A , pp. 641-651
    • Takemura, A.1    Kim, B.H.2
  • 18
    • 0033199056 scopus 로고    scopus 로고
    • Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs
    • Matsubara, T., Ohkubo, N., Andoh T., Sullivan, C. V. and Hara, A. Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev. Biol. 1999; 213:18–32.
    • (1999) Dev. Biol. , vol.213 , pp. 18-32
    • Matsubara, T.1    Ohkubo, N.2    Andoh, T.3    Sullivan, C.V.4    Hara, A.5
  • 19
    • 0016137783 scopus 로고
    • Precursor product relationship between amphibian vitellogenin and the yolk proteins, lipovitellin and phosvitin
    • Bergink, E. W. and Wallace, R. A. Precursor product relationship between amphibian vitellogenin and the yolk proteins, lipovitellin and phosvitin. J. Biol. Chem. 1974; 249(9): 2897–2903.
    • (1974) J. Biol. Chem. , vol.249 , Issue.9 , pp. 2897-2903
    • Bergink, E.W.1    Wallace, R.A.2
  • 20
    • 0017372696 scopus 로고
    • Comparative study of hen yolk phosvitin and plasma vitellogenin
    • Christmann, J. L., Grayson, M. J. and Huang, R. C. C. Comparative study of hen yolk phosvitin and plasma vitellogenin. Biochemistry. 1977; 16: 3250–3256.
    • (1977) Biochemistry. , vol.16 , pp. 3250-3256
    • Christmann, J.L.1    Grayson, M.J.2    Huang, R.C.C.3
  • 21
    • 0029061297 scopus 로고
    • Precursor-product relationship between chicken vitellogenin and the yolk proteins: The 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine-rich domain of vitellogenin II
    • Yamamura, J. I., Adachi, T., Aoki, N., Nakajima, H., Nakamura, R. and Matsuda, T. Precursor-product relationship between chicken vitellogenin and the yolk proteins: The 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine-rich domain of vitellogenin II. Biochim. Biophys. Acta. 1995; 1244 (2–3): 384–394.
    • (1995) Biochim. Biophys. Acta. , vol.1244 , Issue.2-3 , pp. 384-394
    • Yamamura, J.I.1    Adachi, T.2    Aoki, N.3    Nakajima, H.4    Nakamura, R.5    Matsuda, T.6
  • 22
    • 0023656806 scopus 로고
    • Comparison of the organization and fine structure of a chicken and a Xenopus laevis vitellogenin gene
    • Nardelli, D., van het Schip, F. D., Gerber-Huber, S., Haefliger, J. A., Gruber, M., AB, G. and Wahli, W. Comparison of the organization and fine structure of a chicken and a Xenopus laevis vitellogenin gene. J. Biol Chem. 1987; 262(32):15337–15385.
    • (1987) J. Biol Chem. , vol.262 , Issue.32 , pp. 15337-15385
    • Nardelli, D.1    van het Schip, F.D.2    Gerber-Huber, S.3    Haefliger, J.A.4    Gruber, M.5    AB, G.6    Wahli, W.7
  • 23
    • 0000922861 scopus 로고
    • Egg proteins of cofho on (Oncorhynchus kisutch)
    • Markert, J. P. and Vanstone, W. E. Egg proteins of cofho on (Oncorhynchus kisutch). J. Fish. Res. Bd. Can. 1971; 28:1853–1856.
    • (1971) J. Fish. Res. Bd. Can. , vol.28 , pp. 1853-1856
    • Markert, J.P.1    Vanstone, W.E.2
  • 24
    • 0030298341 scopus 로고    scopus 로고
    • Relationship between vitellogenin and its related egg yolk proteins in Sakhalin taimen (Hucho perryi)
    • Hiramatsu, N. and Hara, A. Relationship between vitellogenin and its related egg yolk proteins in Sakhalin taimen (Hucho perryi). Comp. Biochem. Physiol. 1996; 115A: 243–251.
    • (1996) Comp. Biochem. Physiol. , vol.115A , pp. 243-251
    • Hiramatsu, N.1    Hara, A.2
  • 25
    • 0029137432 scopus 로고
    • Proteolytic cleavage of vitellogenin and yolk proteins during vitellogenin uptake and oocyte maturation in barfin flounder (Verasper moseri)
    • Matsubara, T. and Sawano, K. Proteolytic cleavage of vitellogenin and yolk proteins during vitellogenin uptake and oocyte maturation in barfin flounder (Verasper moseri).J. Exp. Zool. 1995; 272: 34–45.
    • (1995) J. Exp. Zool. , vol.272 , pp. 34-45
    • Matsubara, T.1    Sawano, K.2
  • 26
    • 0026437443 scopus 로고
    • Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation
    • Retzek, H., Steyrer, E., Sanders, E. J., Nimpf, J. and Schneider W. J. Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation. DNA Cell Biol. 1992; 11: 661–672.
    • (1992) DNA Cell Biol. , vol.11 , pp. 661-672
    • Retzek, H.1    Steyrer, E.2    Sanders, E.J.3    Nimpf, J.4    Schneider, W.J.5
  • 27
    • 0029936001 scopus 로고    scopus 로고
    • Vitellogenesis-related ovary cathepsin D from Xenopus laevis: purification and properties in comparison with liver cathepsin D
    • Nakamura, K., Yonezawa, S. and Yoshizaki, N. Vitellogenesis-related ovary cathepsin D from Xenopus laevis: purification and properties in comparison with liver cathepsin D. Comp. Biochem. Physiol. 1996; 113B: 835–840.
    • (1996) Comp. Biochem. Physiol. , vol.113B , pp. 835-840
    • Nakamura, K.1    Yonezawa, S.2    Yoshizaki, N.3
  • 28
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire, M. F., Babin, P. J. and Vernier. J. M. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J. Exp. Zool. 1994; 269: 69–83.
    • (1994) J. Exp. Zool. , vol.269 , pp. 69-83
    • Sire, M.F.1    Babin, P.J.2    Vernier, J.M.3
  • 29
    • 21944456030 scopus 로고    scopus 로고
    • Specific proteolysis of vitellogenin to egg yolk proteins in white spotted-charr Salvelinus leucomaenis
    • Hiramatsu, N. and Hara, A. Specific proteolysis of vitellogenin to egg yolk proteins in white spotted-charr Salvelinus leucomaenis. Nippon Suisan Gakkaishi. 1997; 63(5): 701–708.
    • (1997) Nippon Suisan Gakkaishi. , vol.63 , Issue.5 , pp. 701-708
    • Hiramatsu, N.1    Hara, A.2
  • 30
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Spams aurata: involvement of two lysosomal proteinases
    • Carnevali, O., Carletta, R., Cambi, A., Vita, A. and Bromage, N. Yolk formation and degradation during oocyte maturation in seabream Spams aurata: involvement of two lysosomal proteinases. Biol. Reprod. 1999; 60: 140–146.
    • (1999) Biol. Reprod. , vol.60 , pp. 140-146
    • Carnevali, O.1    Carletta, R.2    Cambi, A.3    Vita, A.4    Bromage, N.5
  • 31
    • 85024719116 scopus 로고    scopus 로고
    • Identification and characterization of proteinases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • in press
    • Hiramatsu, N., Ichikawa, N., Fukada, H., Fujita, T., Sullivan, C. V. and Hara, A. Identification and characterization of proteinases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J. Exp. Zool. 2001; 290 (in press).
    • (2001) J. Exp. Zool. , pp. 290
    • Hiramatsu, N.1    Ichikawa, N.2    Fukada, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 32
    • 0022244976 scopus 로고
    • Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological considerations
    • Wallace, R. A. and Begovac, P. C. Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological considerations. J. Biol. Chem. 1985; 260:11268–11274.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11268-11274
    • Wallace, R.A.1    Begovac, P.C.2
  • 33
    • 0022416087 scopus 로고
    • Major protein changes during vitellogenesis and maturation of Fundulus oocytes
    • Wallace, R. A. and Selman, K. Major protein changes during vitellogenesis and maturation of Fundulus oocytes. Dev. Biol. 1985; 110: 492–498.
    • (1985) Dev. Biol. , vol.110 , pp. 492-498
    • Wallace, R.A.1    Selman, K.2
  • 34
    • 0022595211 scopus 로고
    • Changes in teleost yolk proteins during oocyte maturation: Correlation of yolk proteolysis with oocyte hydration
    • Greeley, M. S., Jr., Calder, D. R. and Wallace, R. A. Changes in teleost yolk proteins during oocyte maturation: Correlation of yolk proteolysis with oocyte hydration. Comp. Biochem. Physiol. 1986; 84B, 1–9.
    • (1986) Comp. Biochem. Physiol. , vol.84B , pp. 1-9
    • Greeley, M.S.1    Calder, D.R.2    Wallace, R.A.3
  • 35
    • 85008131860 scopus 로고
    • Changes of lipovitellin during in vitro oocyte maturation in Japanese flounder, Paralichthys olivaceus
    • Matusbara, T., Adachi, S., Ijiri, S. and Yamauchi, K. Changes of lipovitellin during in vitro oocyte maturation in Japanese flounder, Paralichthys olivaceus. Fish. Sci. 1995;61:478–481.
    • (1995) Fish. Sci. , vol.61 , pp. 478-481
    • Matusbara, T.1    Adachi, S.2    Ijiri, S.3    Yamauchi, K.4
  • 36
    • 0026014493 scopus 로고
    • Changes in size, hydration and low molecular weight osmotic effectors during meiotic maturation of Fundulus oocytes in vivo
    • Greeley, M. S., Jr., Hols, H. and Wallace, R. A. Changes in size, hydration and low molecular weight osmotic effectors during meiotic maturation of Fundulus oocytes in vivo. Comp. Biochem. Physiol. 1991; 100A: 639–647.
    • (1991) Comp. Biochem. Physiol. , vol.100A , pp. 639-647
    • Greeley, M.S.1    Hols, H.2    Wallace, R.A.3
  • 37
    • 0030174260 scopus 로고    scopus 로고
    • Final oocyte maturation in vivo and in vitro in marine fishes with pelagic eggs: Yolk protein hydrolysis and free amino acid content
    • Thorsen, A. and Fyhn, H. J. Final oocyte maturation in vivo and in vitro in marine fishes with pelagic eggs: Yolk protein hydrolysis and free amino acid content. J. Fish. Biol. 1996; 48:1195–1209.
    • (1996) J. Fish. Biol. , vol.48 , pp. 1195-1209
    • Thorsen, A.1    Fyhn, H.J.2
  • 38
    • 0038447050 scopus 로고    scopus 로고
    • Course of proteolytic cleavage in three classes of yolk proteins during oocyte maturation in barfin flounder (Varasper moseri)
    • Matsubara, T. and Koya, Y. Course of proteolytic cleavage in three classes of yolk proteins during oocyte maturation in barfin flounder (Varasper moseri). J. Exp. Zool. 1997; 272: 34–45.
    • (1997) J. Exp. Zool. , vol.272 , pp. 34-45
    • Matsubara, T.1    Koya, Y.2
  • 39
    • 0029052706 scopus 로고
    • Respiration, nitrogen and energy metabolism of developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus L.)
    • Finn, R. N., Ronnestad, I. and Fyhn, H. J. Respiration, nitrogen and energy metabolism of developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus L.). Comp. Biochem. Physiol. 1995; 111A: 647–671.
    • (1995) Comp. Biochem. Physiol. , vol.111A , pp. 647-671
    • Finn, R.N.1    Ronnestad, I.2    Fyhn, H.J.3
  • 40
    • 0035870296 scopus 로고    scopus 로고
    • Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Malanogrammus aeglefinus)
    • Reith, M., Munholland, J., Kelly, J., Finn, R. N. and Fyhn, H. J. Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Malanogrammus aeglefinus). J. Exp. Zool. 2001;291:58–67.
    • (2001) J. Exp. Zool. , vol.291 , pp. 58-67
    • Reith, M.1    Munholland, J.2    Kelly, J.3    Finn, R.N.4    Fyhn, H.J.5
  • 41
    • 0028021642 scopus 로고
    • Plasma levels of gonadal steroids during final oocyte maturation of striped bass, Morone saxatilis
    • King, W. V., Thomas, P., Harrell, R. M., Hodson, R. G. and Su llivan, C. V. Plasma levels of gonadal steroids during final oocyte maturation of striped bass, Morone saxatilis. Gen. Com. Endcrinol. 1994; 95: 178–191.
    • (1994) Gen. Com. Endcrinol. , vol.95 , pp. 178-191
    • King, W.V.1    Thomas, P.2    Harrell, R.M.3    Hodson, R.G.4    Su llivan, C.V.5
  • 42
    • 0035421972 scopus 로고    scopus 로고
    • Bafilomycin Al inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes
    • Selman, K., Wallace, R. A. and Cerda, J. Bafilomycin Al inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes. J. Exp. Zool. 2001; 290: 265–278.
    • (2001) J. Exp. Zool. , vol.290 , pp. 265-278
    • Selman, K.1    Wallace, R.A.2    Cerda, J.3
  • 43
    • 85024725910 scopus 로고    scopus 로고
    • Sequential utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of barfin flounder Verasper moseri
    • in press
    • Ohkubo, N. and Matsubara, T. Sequential utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of barfin flounder Verasper moseri. Marine Biology 2001; (in press).
    • (2001) Marine Biology
    • Ohkubo, N.1    Matsubara, T.2
  • 44
    • 0000782872 scopus 로고
    • Yolk proteins in salmon (Salmo salar) oocytes, eyed eggs, and alevins differing in viability
    • Olin, T. and Von Der Decken, A. Yolk proteins in salmon (Salmo salar) oocytes, eyed eggs, and alevins differing in viability. Can. J. Zool. 1990; 68: 895–900.
    • (1990) Can. J. Zool. , vol.68 , pp. 895-900
    • Olin, T.1    Von Der Decken, A.2
  • 45
    • 0033230418 scopus 로고    scopus 로고
    • Developmental fate of the yolk protein lipovitellin in embryos and larvae of winter flounder, Pleuronectes americanus
    • Hartling, R. C. and Kunkel, J. G. Developmental fate of the yolk protein lipovitellin in embryos and larvae of winter flounder, Pleuronectes americanus. J. Exp. Zool. 1999; 284: 686–695.
    • (1999) J. Exp. Zool. , vol.284 , pp. 686-695
    • Hartling, R.C.1    Kunkel, J.G.2
  • 46
    • 0028569571 scopus 로고
    • The wildlife/human connection: modernizing risk decisions
    • 102 SuppI
    • Colborn, T. The wildlife/human connection: modernizing risk decisions. Environ. Health Perspect. 1994; 102 SuppI 12: 55–59.
    • (1994) Environ. Health Perspect. , vol.12 , pp. 55-59
    • Colborn, T.1
  • 47
    • 0028840615 scopus 로고
    • Vitellogenesis as a biomarker for estrogenic contamination of the aquatic environment
    • Sumpter, J. P. and Jobling, S. Vitellogenesis as a biomarker for estrogenic contamination of the aquatic environment. Environ. Helth Perspect. 1995; 103: 173–178.
    • (1995) Environ. Helth Perspect. , vol.103 , pp. 173-178
    • Sumpter, J.P.1    Jobling, S.2
  • 49
    • 0029854519 scopus 로고    scopus 로고
    • Vitellogenin induction and reduced serum testosterone concentrations in feral male carp (Cyprinus carpio) captured near a major metropolitan sewage treatment plant
    • Folmer, L. C., Denslow, N. D., Rao, V., Chow, M., Crain, D. A., Enblom, J., Marcino, J. and Guillette, Jr., L. J. Vitellogenin induction and reduced serum testosterone concentrations in feral male carp (Cyprinus carpio) captured near a major metropolitan sewage treatment plant. Environ. Health Perspect. 1996; 104:1096–1101.
    • (1996) Environ. Health Perspect. , vol.104 , pp. 1096-1101
    • Folmer, L.C.1    Denslow, N.D.2    Rao, V.3    Chow, M.4    Crain, D.A.5    Enblom, J.6    Marcino, J.7    Guillette, L.J.8
  • 51
    • 0029138877 scopus 로고
    • A highly conserved N-terminal sequence for teleost vitellogenin with potential value to the biochemistry, molecular biology and pathology of vitellogenesis
    • Folmar, L. C., Denslow, N. D., Wallace, R. A., LaFleur, G. J., Gross, T. S., Bonomelli, S. and Sullivan, C. V. A highly conserved N-terminal sequence for teleost vitellogenin with potential value to the biochemistry, molecular biology and pathology of vitellogenesis. J. Fish Biol. 1995; 46: 255–263.
    • (1995) J. Fish Biol. , vol.46 , pp. 255-263
    • Folmar, L.C.1    Denslow, N.D.2    Wallace, R.A.3    LaFleur, G.J.4    Gross, T.S.5    Bonomelli, S.6    Sullivan, C.V.7
  • 53
    • 0002489180 scopus 로고    scopus 로고
    • Vitellogenin in wild male flounder, Pleuronectes yokohamae, in Tokyo bay, Japan
    • Hashimoto, S. Bessho, H., Sato, K., Hara, A. and Fujita, K. Vitellogenin in wild male flounder, Pleuronectes yokohamae, in Tokyo bay, Japan. Jpn. J. Environ. Toxicol. 1998; 1: 75–85.
    • (1998) Jpn. J. Environ. Toxicol. , vol.1 , pp. 75-85
    • Hashimoto, S.1    Bessho, H.2    Sato, K.3    Hara, A.4    Fujita, K.5
  • 55
  • 56
    • 0034906760 scopus 로고    scopus 로고
    • Development and validation of chemi-luminescent immunoassay for vitellogenin in five salmonid species
    • Fukada, H., Haga, A., Fujita, T., Hiramatsu, N., Sullivan, C. V. and Hara, A. Development and validation of chemi-luminescent immunoassay for vitellogenin in five salmonid species. Comp. Biochem. Physiol. 2001; 130A: 163–170.
    • (2001) Comp. Biochem. Physiol. , vol.130A , pp. 163-170
    • Fukada, H.1    Haga, A.2    Fujita, T.3    Hiramatsu, N.4    Sullivan, C.V.5    Hara, A.6


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