메뉴 건너뛰기




Volumn 128, Issue 2, 1997, Pages 213-224

Ultrastructure of the vitelline coat in the ascidians Phallusia mammillata, Ascidia mentula and Ciona intestinalis: New aspects revealed by freeze-substitution and deep-etching

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0030967367     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002270050085     Document Type: Article
Times cited : (16)

References (64)
  • 1
    • 0019951687 scopus 로고
    • Glucosaminoglycans in bovine cumulus-oocyte complexes: Morphology and chemistry
    • Ball GD, Bellin ME, Ax RL, First NL (1982) Glucosaminoglycans in bovine cumulus-oocyte complexes: morphology and chemistry. Molec cell Endocr 28: 113-122
    • (1982) Molec Cell Endocr , vol.28 , pp. 113-122
    • Ball, G.D.1    Bellin, M.E.2    Ax, R.L.3    First, N.L.4
  • 2
    • 0001854478 scopus 로고
    • Studies in tunicate development. Part I. General physiology of development of simple ascidians
    • Ser B
    • Berrill NJ (1929) Studies in tunicate development. Part I. General physiology of development of simple ascidians. Phil Trans R Soc (Ser B) 218: 37-78
    • (1929) Phil Trans R Soc , vol.218 , pp. 37-78
    • Berrill, N.J.1
  • 3
    • 0029898922 scopus 로고    scopus 로고
    • Egg jelly layers of Xenopus laevis are unique in ultrastructure and sugar distribution
    • Bonnell BS, Chandler DE (1996) Egg jelly layers of Xenopus laevis are unique in ultrastructure and sugar distribution. Molec Reprod Dev 44: 212-220
    • (1996) Molec Reprod Dev , vol.44 , pp. 212-220
    • Bonnell, B.S.1    De Chandler2
  • 4
    • 0028230518 scopus 로고
    • The sea urchin egg jelly coat consists of globular glycoproteins bound to a fibrous fucan superstructure
    • Bonnell BS, Keller SH, Vacquier VD, Chandler DE (1994) The sea urchin egg jelly coat consists of globular glycoproteins bound to a fibrous fucan superstructure. Devl Biol 162: 313-324
    • (1994) Devl Biol , vol.162 , pp. 313-324
    • Bonnell, B.S.1    Keller, S.H.2    Vacquier, V.D.3    Chandler, D.E.4
  • 5
    • 0027192869 scopus 로고
    • The sea urchin egg jelly coat is a three-dimensional fibrous network as seen by intermediate voltage electron microscopy and deep etching analysis
    • Bonnell BS, Larabell C, Chandler DE (1993) The sea urchin egg jelly coat is a three-dimensional fibrous network as seen by intermediate voltage electron microscopy and deep etching analysis. Molec Reprod Dev 35: 181-188
    • (1993) Molec Reprod Dev , vol.35 , pp. 181-188
    • Bonnell, B.S.1    Larabell, C.2    Chandler, D.E.3
  • 6
    • 84984042882 scopus 로고
    • Volumenveränderungen biologischer Gewebe bei Entwässerung und Trocknung
    • Pfefferkorn G (ed) Kommissionsverlag Remy, Muenster
    • Boyde A (1978) Volumenveränderungen biologischer Gewebe bei Entwässerung und Trocknung. In: Pfefferkorn G (ed) Beiträge zur elektronenmikroskopischen Direktabbildung von Oberflächen, BEDO (11). Kommissionsverlag Remy, Muenster, pp 231-242
    • (1978) Beiträge zur Elektronenmikroskopischen Direktabbildung von Oberflächen, BEDO (11) , pp. 231-242
    • Boyde, A.1
  • 7
    • 0026695427 scopus 로고
    • Preservation and visualization of the sea urchin embryo blastocoelic extracellular matrix
    • Cherr GN, Summers RG, Baldwin JD, Morrill JB (1992) Preservation and visualization of the sea urchin embryo blastocoelic extracellular matrix. Microscopy Res Technique 22(1): 11-22
    • (1992) Microscopy Res Technique , vol.22 , Issue.1 , pp. 11-22
    • Cherr, G.N.1    Summers, R.G.2    Baldwin, J.D.3    Morrill, J.B.4
  • 8
    • 0025035969 scopus 로고
    • Organization of the hamster cumulus extracellular matrix: A hyaluronate-glycoprotein gel which modulates sperm access to the oocyte
    • Cherr GN, Yudin AI, Katz DF (1990) Organization of the hamster cumulus extracellular matrix: a hyaluronate-glycoprotein gel which modulates sperm access to the oocyte. Dev Growth Differentiation 32(4): 353-365
    • (1990) Dev Growth Differentiation , vol.32 , Issue.4 , pp. 353-365
    • Cherr, G.N.1    Yudin, A.I.2    Katz, D.F.3
  • 9
    • 0019865507 scopus 로고
    • Differentiation of the vitelline coat in the ascidian Ciona intestinalis: An ultrastructural study
    • Cotelli F, Andronico F, De Santis R, Monroy A, Rosati F (1981) Differentiation of the vitelline coat in the ascidian Ciona intestinalis: an ultrastructural study. Wilhelm Roux Arch dev Biol 190: 252-258
    • (1981) Wilhelm Roux Arch Dev Biol , vol.190 , pp. 252-258
    • Cotelli, F.1    Andronico, F.2    De Santis, R.3    Monroy, A.4    Rosati, F.5
  • 10
    • 0018895683 scopus 로고
    • A study of the chorion and the follicle cells in relation to the sperm-egg interaction in the ascidian, Ciona intestinalis
    • De Santis R, Jamunno G, Rosati F (1980) A study of the chorion and the follicle cells in relation to the sperm-egg interaction in the ascidian, Ciona intestinalis. Devl Biol 74: 490-499
    • (1980) Devl Biol , vol.74 , pp. 490-499
    • De Santis, R.1    Jamunno, G.2    Rosati, F.3
  • 12
    • 0000400726 scopus 로고
    • Morphological aspects of ascidian fertilization: Acrosome reaction, apical processes and gamete fusion in Ciona intestinalis
    • Fukumoto M (1990) Morphological aspects of ascidian fertilization: acrosome reaction, apical processes and gamete fusion in Ciona intestinalis. Invert Reprod Dev 17(2): 147-154
    • (1990) Invert Reprod Dev , vol.17 , Issue.2 , pp. 147-154
    • Fukumoto, M.1
  • 13
    • 0027217779 scopus 로고
    • Morphological aspects of fertilization in Phallusia (Ascidia) nigra (Ascidiacea, Tunicata)
    • Fukumoto M (1993) Morphological aspects of fertilization in Phallusia (Ascidia) nigra (Ascidiacea, Tunicata). Wilhelm Roux Arch dev Biol 202: 321-328
    • (1993) Wilhelm Roux Arch Dev Biol , vol.202 , pp. 321-328
    • Fukumoto, M.1
  • 14
    • 0029126777 scopus 로고
    • Morphological aspects of fertilization in Halocynthia roretzi (Ascidiacea, Tunicata)
    • Fukumoto M (1995) Morphological aspects of fertilization in Halocynthia roretzi (Ascidiacea, Tunicata). J struct Biol 114: 157-166
    • (1995) J Struct Biol , vol.114 , pp. 157-166
    • Fukumoto, M.1
  • 15
    • 21144480796 scopus 로고
    • The acrosome and its differentiation during spermiogenesis in Halocynthia roretzi (Ascidiacea, Tunicata)
    • Fukumoto M, Numakunai T (1993) The acrosome and its differentiation during spermiogenesis in Halocynthia roretzi (Ascidiacea, Tunicata). Zool Sci 10: 103-109
    • (1993) Zool Sci , vol.10 , pp. 103-109
    • Fukumoto, M.1    Numakunai, T.2
  • 16
    • 0022653966 scopus 로고
    • Advances in ultrarapid freezing for the preservation of cellular ultrastructure
    • Gilkey JC, Staehelin LA (1986) Advances in ultrarapid freezing for the preservation of cellular ultrastructure. J Electron Microscopy Tech 3: 177-210
    • (1986) J Electron Microscopy Tech , vol.3 , pp. 177-210
    • Gilkey, J.C.1    Staehelin, L.A.2
  • 17
    • 0026087535 scopus 로고
    • Isolation, characterization, and localization of a sperm-bound N-acetylglucosaminidase that is indispensable for fertilization in the ascidian, Phallusia mammillata
    • Godknecht A, Honegger TG (1991) Isolation, characterization, and localization of a sperm-bound N-acetylglucosaminidase that is indispensable for fertilization in the ascidian, Phallusia mammillata. Devl Biol 143: 398-407
    • (1991) Devl Biol , vol.143 , pp. 398-407
    • Godknecht, A.1    Honegger, T.G.2
  • 18
    • 0023139144 scopus 로고
    • Mammalian sperm cannot penetrate the zona pellucida solely by force
    • Green DPL (1987) Mammalian sperm cannot penetrate the zona pellucida solely by force. Expl Cell Res 169: 31-38
    • (1987) Expl Cell Res , vol.169 , pp. 31-38
    • Green, D.P.L.1
  • 19
    • 0021235172 scopus 로고
    • Mechanical hypothesis of sperm penetration
    • Green DPL, Purves RD (1984) Mechanical hypothesis of sperm penetration. Biophys J 45(4): 659-662
    • (1984) Biophys J , vol.45 , Issue.4 , pp. 659-662
    • Green, D.P.L.1    Purves, R.D.2
  • 20
    • 0027414416 scopus 로고
    • Impact of freeze substitution on biological electron microscopy
    • Hippe-Sanwald S (1993) Impact of freeze substitution on biological electron microscopy. Microscopy Res Technique 24: 400-422
    • (1993) Microscopy Res Technique , vol.24 , pp. 400-422
    • Hippe-Sanwald, S.1
  • 21
    • 0023001824 scopus 로고
    • Fertilization in ascidians: Studies on the egg envelope, sperm and gamete interactions in Phallusia mammillata
    • Honegger TG (1986) Fertilization in ascidians: studies on the egg envelope, sperm and gamete interactions in Phallusia mammillata. Devl Biol 118: 118-128
    • (1986) Devl Biol , vol.118 , pp. 118-128
    • Honegger, T.G.1
  • 22
    • 0002354840 scopus 로고
    • Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in ascidians
    • Hedrick JL (ed) Plenum Press, New York
    • Hoshi M (1984) Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in ascidians. In: Hedrick JL (ed) The molecular and cellular biology of fertilization. Plenum Press, New York, pp 251-260
    • (1984) The Molecular and Cellular Biology of Fertilization , pp. 251-260
    • Hoshi, M.1
  • 23
    • 0001051185 scopus 로고
    • Glycosidases, proteases and ascidian fertilization
    • Hoshi M, Takizawa S, Hirohashi N (1994) Glycosidases, proteases and ascidian fertilization. Semin devl Biol 5: 201-208
    • (1994) Semin Devl Biol , vol.5 , pp. 201-208
    • Hoshi, M.1    Takizawa, S.2    Hirohashi, N.3
  • 26
    • 84985824006 scopus 로고
    • Cytological characterization of self incompatability in gametes of the ascidian, Ciona interstinalis
    • Kawamura K, Fujita H, Nakauchi M (1987) Cytological characterization of self incompatability in gametes of the ascidian, Ciona interstinalis. Dev Growth Differentiation 29(6): 627-642
    • (1987) Dev Growth Differentiation , vol.29 , Issue.6 , pp. 627-642
    • Kawamura, K.1    Fujita, H.2    Nakauchi, M.3
  • 27
    • 0002724650 scopus 로고
    • The response of biological macromolecules and supramolecular structures to the physics of specimen cryopreservation
    • Steinbrecht RA, Zierold K (eds) Springer-Verlag, Berlin
    • Kellenberger E (1987) The response of biological macromolecules and supramolecular structures to the physics of specimen cryopreservation. In: Steinbrecht RA, Zierold K (eds) Cryotechniques in biological electron microscopy. Springer-Verlag, Berlin, pp 35-63
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 35-63
    • Kellenberger, E.1
  • 28
    • 0028331539 scopus 로고
    • The isolation of acrosome-reaction-inducing glycoproteins from sea urchin egg jelly
    • Keller SH, Vacquier VD (1994) The isolation of acrosome-reaction-inducing glycoproteins from sea urchin egg jelly. Devl Biol 162: 304-312
    • (1994) Devl Biol , vol.162 , pp. 304-312
    • Keller, S.H.1    Vacquier, V.D.2
  • 29
    • 1842413902 scopus 로고
    • Structure of the ascidian vitelline coat and its role in fertilization
    • Koch RA, Johnson JS, Lambert CC (1993) Structure of the ascidian vitelline coat and its role in fertilization. J Reprod Dev 39 (Suppl): 35-36
    • (1993) J Reprod Dev , vol.39 , Issue.SUPPL. , pp. 35-36
    • Koch, R.A.1    Johnson, J.S.2    Lambert, C.C.3
  • 30
    • 0025102016 scopus 로고
    • Ultrastructure of sperm, spermiogenesis, and sperm egg interactions in selected invertebrates and lower vertebrates which use external fertilization
    • Koch RA, Lambert CC (1990) Ultrastructure of sperm, spermiogenesis, and sperm egg interactions in selected invertebrates and lower vertebrates which use external fertilization. J Electron Microscopy Tech 16: 115-154
    • (1990) J Electron Microscopy Tech , vol.16 , pp. 115-154
    • Koch, R.A.1    Lambert, C.C.2
  • 31
    • 0028349681 scopus 로고
    • Sperm-surface chymotrypsin-like protease activity required for fertilization in ascidians
    • Koch RA, Norton ML, Vazquez H, Lambert CC (1994) Sperm-surface chymotrypsin-like protease activity required for fertilization in ascidians. Devl Biol 162: 438-450
    • (1994) Devl Biol , vol.162 , pp. 438-450
    • Koch, R.A.1    Norton, M.L.2    Vazquez, H.3    Lambert, C.C.4
  • 32
    • 1842315646 scopus 로고
    • The ascidian sperm reaction
    • Lambert CC (1982) The ascidian sperm reaction. Am Zool 22(4): 841-849
    • (1982) Am Zool , vol.22 , Issue.4 , pp. 841-849
    • Lambert, C.C.1
  • 33
    • 0001249446 scopus 로고
    • Fertilization-induced modification of chorion N-acetylglucosamine groups blocks polyspermy in ascidian eggs
    • Lambert CC (1986) Fertilization-induced modification of chorion N-acetylglucosamine groups blocks polyspermy in ascidian eggs. Devl Biol 116: 168-173
    • (1986) Devl Biol , vol.116 , pp. 168-173
    • Lambert, C.C.1
  • 34
    • 0018350052 scopus 로고
    • Calcium-mediated mitochondrial movement in ascidian sperm during fertilization
    • Lambert CC, Epel D (1979) Calcium-mediated mitochondrial movement in ascidian sperm during fertilization. Devl Biol 69: 296-304
    • (1979) Devl Biol , vol.69 , pp. 296-304
    • Lambert, C.C.1    Epel, D.2
  • 35
    • 0026476428 scopus 로고
    • Glycolipid linkage of a polyspermy blocking glycosidase to the ascidian egg surface
    • Lambert CC, Goode CA (1992) Glycolipid linkage of a polyspermy blocking glycosidase to the ascidian egg surface. Devl Biol 154: 95-100
    • (1992) Devl Biol , vol.154 , pp. 95-100
    • Lambert, C.C.1    Goode, C.A.2
  • 36
    • 84985793280 scopus 로고
    • Sperm binding and penetration during ascidian fertilization
    • Lambert CC, Koch RA (1988) Sperm binding and penetration during ascidian fertilization. Dev Growth Differentiation 30: 325-336
    • (1988) Dev Growth Differentiation , vol.30 , pp. 325-336
    • Lambert, C.C.1    Koch, R.A.2
  • 37
    • 0021674071 scopus 로고
    • The role of actin and myosin in ascidian sperm mitochondrial translocation
    • Lambert CC, Lambert G (1984) The role of actin and myosin in ascidian sperm mitochondrial translocation. Devl Biol 106: 307-314
    • (1984) Devl Biol , vol.106 , pp. 307-314
    • Lambert, C.C.1    Lambert, G.2
  • 38
    • 0024505215 scopus 로고
    • The coelomic envelope of Xenopus laevis eggs: A quick-freeze, deep-etch analysis
    • Larabell CA, Chandler DE (1989) The coelomic envelope of Xenopus laevis eggs: a quick-freeze, deep-etch analysis. Devl Biol 131: 126-135
    • (1989) Devl Biol , vol.131 , pp. 126-135
    • Larabell, C.A.1    Chandler, D.E.2
  • 39
    • 0001777551 scopus 로고
    • A critical appraisal of the effects of fixation, dehydration and embedding on cell volume
    • Revel JP, Barnard T, Haggis GH (eds) SEM Inc., AMF O'Hare
    • Lee RMKW (1984) A critical appraisal of the effects of fixation, dehydration and embedding on cell volume. In: Revel JP, Barnard T, Haggis GH (eds) The science of biological specimen preparation. SEM Inc., AMF O'Hare, pp 61-70
    • (1984) The Science of Biological Specimen Preparation , pp. 61-70
    • Lee, R.M.K.W.1
  • 41
    • 0026346112 scopus 로고
    • Glycoprotein constituents of the vitelline coat of Phallusia mammillata (Ascidiacea) with fertilization inhibiting activity
    • Litscher E, Honegger TG (1991) Glycoprotein constituents of the vitelline coat of Phallusia mammillata (Ascidiacea) with fertilization inhibiting activity. Devl Biol 148: 536-551
    • (1991) Devl Biol , vol.148 , pp. 536-551
    • Litscher, E.1    Honegger, T.G.2
  • 42
    • 3643092789 scopus 로고
    • Test cells of Ascidiella aspersa: Adhesion and migration behaviour during embryogenesis
    • Lübbering B, Niermann-Kerkenberg E, Hofmann DK (1992) Test cells of Ascidiella aspersa: adhesion and migration behaviour during embryogenesis. Invert Reprod Dev 21(3): 241-252
    • (1992) Invert Reprod Dev , vol.21 , Issue.3 , pp. 241-252
    • Lübbering, B.1    Niermann-Kerkenberg, E.2    Hofmann, D.K.3
  • 43
    • 0026655040 scopus 로고
    • Purification and characterization of a vitelline coat lysin from Ciona intestinalis spermatozoa
    • Marino R, De Santis R, Hirohashi N, Hoshi M, Pinto MR, Usui N (1992) Purification and characterization of a vitelline coat lysin from Ciona intestinalis spermatozoa. Molec Reprod Dev 32: 383-388
    • (1992) Molec Reprod Dev , vol.32 , pp. 383-388
    • Marino, R.1    De Santis, R.2    Hirohashi, N.3    Hoshi, M.4    Pinto, M.R.5    Usui, N.6
  • 44
    • 0027131784 scopus 로고
    • Purification and properties of N-acetylglucosaminidase from eggs of the ascidian, Halocynthia roretzi
    • Matsuura K, Sawada H, Yokosawa H (1993) Purification and properties of N-acetylglucosaminidase from eggs of the ascidian, Halocynthia roretzi. Eur J Biochem 218: 535-541
    • (1993) Eur J Biochem , vol.218 , pp. 535-541
    • Matsuura, K.1    Sawada, H.2    Yokosawa, H.3
  • 46
    • 0344373583 scopus 로고
    • Interspecific fertilization in ascidians
    • Minganti A (1948) Interspecific fertilization in ascidians. Nature, Lond 161: 643-644
    • (1948) Nature, Lond , vol.161 , pp. 643-644
    • Minganti, A.1
  • 47
    • 1842286146 scopus 로고
    • Events at the cell surface: Exocytosis and remodeling of the extracellular matrix as seen in quick-frozen, deep-etched cells
    • Severs NJ, Shotton DM (eds) Wiley-Liss, New York
    • Mozingo NM, Chandler DE (1995) Events at the cell surface: exocytosis and remodeling of the extracellular matrix as seen in quick-frozen, deep-etched cells. In: Severs NJ, Shotton DM (eds) Rapid freezing, freeze fracture, and deep etching. Wiley-Liss, New York, pp 285-309
    • (1995) Rapid Freezing, Freeze Fracture, and Deep Etching , pp. 285-309
    • Mozingo, N.M.1    Chandler, D.E.2
  • 48
    • 0029119174 scopus 로고
    • Structural features of the abalone egg extracellular matrix and its role in gamete interaction during fertilization
    • Mozingo NM, Vacquier VD, Chandler DE (1995) Structural features of the abalone egg extracellular matrix and its role in gamete interaction during fertilization. Molec Reprod Dev 41: 493-502
    • (1995) Molec Reprod Dev , vol.41 , pp. 493-502
    • Mozingo, N.M.1    Vacquier, V.D.2    Chandler, D.E.3
  • 49
    • 0019559240 scopus 로고
    • Studies on fertilization in the ascidians: Fucosyl sites on vitelline coat of Ciona intestinalis
    • Pinto MR, De Santis R, D'Alessio G, Rosati F (1981) Studies on fertilization in the ascidians: fucosyl sites on vitelline coat of Ciona intestinalis. Expl Cell Res 132: 289-295
    • (1981) Expl Cell Res , vol.132 , pp. 289-295
    • Pinto, M.R.1    De Santis, R.2    D'Alessio, G.3    Rosati, F.4
  • 50
    • 0029069402 scopus 로고
    • Specific induction of self-discrimination by follicle cells in Ciona intestinalis oocytes
    • Pinto MR, De Santis R, Marino R, Usui N (1995) Specific induction of self-discrimination by follicle cells in Ciona intestinalis oocytes. Dev Growth Differentiation 37: 287-291
    • (1995) Dev Growth Differentiation , vol.37 , pp. 287-291
    • Pinto, M.R.1    De Santis, R.2    Marino, R.3    Usui, N.4
  • 51
    • 1542431022 scopus 로고
    • Cryofixation of biological materials for electron microscopy by the methods of spray-, sandwich-, cry-, ogen-jet-, and sandwich-cryogen-jet-freezing: A comparison of techniques
    • Revel JP, Barnard T, Haggis GH (eds) SEM Inc., AMF O'Hare
    • Plattner H, Knoll G (1984) Cryofixation of biological materials for electron microscopy by the methods of spray-, sandwich-, cry-, ogen-jet-, and sandwich-cryogen-jet-freezing: a comparison of techniques. In: Revel JP, Barnard T, Haggis GH (eds) The science of biological specimen preparation. SEM Inc., AMF O'Hare, pp 139-146
    • (1984) The Science of Biological Specimen Preparation , pp. 139-146
    • Plattner, H.1    Knoll, G.2
  • 52
    • 0017817267 scopus 로고
    • Studies on fertilization in the ascidians, I. Self sterility and specific recognition between gametes of Ciona intestinalis
    • Rosati F, De Santis R (1978) Studies on fertilization in the ascidians, I. Self sterility and specific recognition between gametes of Ciona intestinalis. Expl Cell Res 112: 111-119
    • (1978) Expl Cell Res , vol.112 , pp. 111-119
    • Rosati, F.1    De Santis, R.2
  • 53
    • 0018172555 scopus 로고
    • Studies on fertilization in the ascidians. II. Lectin binding to the gametes of Ciona intestinalis
    • Rosati F, De Santis R, Monroy A (1978) Studies on fertilization in the ascidians. II. Lectin binding to the gametes of Ciona intestinalis. Expl Cell Res 116: 419-427
    • (1978) Expl Cell Res , vol.116 , pp. 419-427
    • Rosati, F.1    De Santis, R.2    Monroy, A.3
  • 54
    • 0001580678 scopus 로고
    • A modified method for lead staining of thin sections
    • Sato T (1967) A modified method for lead staining of thin sections. J Electron Microscopy 16(2): p 193
    • (1967) J Electron Microscopy , vol.16 , Issue.2 , pp. 193
    • Sato, T.1
  • 55
    • 0030585338 scopus 로고    scopus 로고
    • Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease
    • Sawada H, Iwasaki K, Kihara-Negishi F, Ariga H, Yokosawa H (1996) Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease. Biochem biophys Res Commun 222: 499-504
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 499-504
    • Sawada, H.1    Iwasaki, K.2    Kihara-Negishi, F.3    Ariga, H.4    Yokosawa, H.5
  • 56
    • 0022345489 scopus 로고
    • Trypsin-like enzyme from eggs of the ascidian (protochordate), Halocynthia roretzi
    • Sawada H, Kawahigashi M, Yokosawa H, Ishii S (1985) Trypsin-like enzyme from eggs of the ascidian (protochordate), Halocynthia roretzi. J biol Chem 260 (29): 15694-15698
    • (1985) J Biol Chem , vol.260 , Issue.29 , pp. 15694-15698
    • Sawada, H.1    Kawahigashi, M.2    Yokosawa, H.3    Ishii, S.4
  • 57
    • 0021759356 scopus 로고
    • Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi
    • Sawada H, Yokosawa H, Ishii S (1984) Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi. J biol Chem 259 (5): 2900-2904
    • (1984) J Biol Chem , vol.259 , Issue.5 , pp. 2900-2904
    • Sawada, H.1    Yokosawa, H.2    Ishii, S.3
  • 58
    • 0025148154 scopus 로고
    • Common sense in electron microscopy: About cryofixation, freeze-substitution, low temperature embedding, and low denaturation embedding
    • Sjöstrand FS (1990) Common sense in electron microscopy: about cryofixation, freeze-substitution, low temperature embedding, and low denaturation embedding. J struct Biol 103: 135-139
    • (1990) J Struct Biol , vol.103 , pp. 135-139
    • Sjöstrand, F.S.1
  • 59
    • 0014444144 scopus 로고
    • A low-viscosity epoxy resin embedding medium for electron microscopy
    • Spurr AR (1969) A low-viscosity epoxy resin embedding medium for electron microscopy. J Ultrastruct Res 26: 31-43
    • (1969) J Ultrastruct Res , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 60
    • 0002743936 scopus 로고
    • Freeze-substitution and freeze-drying
    • Steinbrecht RA, Zierold K (eds) Springer-Verlag, Berlin
    • Steinbrecht RA, Müller M (1987) Freeze-substitution and freeze-drying. In: Steinbrecht RA, Zierold K (eds) Cryotechniques in biological electron microscopy. Springer-Verlag, Berlin, pp 149-172
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 149-172
    • Steinbrecht, R.A.1    Müller, M.2
  • 63
    • 0038886681 scopus 로고
    • Ultrastructural investigations on sperm penetration and gamete fusion in the ascidians Boltenia villosa and Phallusia mammillata
    • Xie M, Honegger TG (1993) Ultrastructural investigations on sperm penetration and gamete fusion in the ascidians Boltenia villosa and Phallusia mammillata. Mar Biol 116: 117-127
    • (1993) Mar Biol , vol.116 , pp. 117-127
    • Xie, M.1    Honegger, T.G.2
  • 64
    • 0023871247 scopus 로고
    • Structure of the cumulus matrix and zona pellucida in the golden hamster: A new view of sperm interaction with oocyte-associated extracellular matrices
    • Yudin AI, Cherr GN, Katz DF (1988) Structure of the cumulus matrix and zona pellucida in the golden hamster: a new view of sperm interaction with oocyte-associated extracellular matrices. Cell Tissue Res 251: 555-564
    • (1988) Cell Tissue Res , vol.251 , pp. 555-564
    • Yudin, A.I.1    Cherr, G.N.2    Katz, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.