메뉴 건너뛰기




Volumn 6, Issue 1, 1998, Pages 1-9

Immunohistochemical localisation of a galectin from Bufo arenarum ovary

Author keywords

Bufo arenarum; Galectin; Immunohistochemistry; Ovary; Toad

Indexed keywords

ANIMALIA; ANURA; BUFO ARENARUM;

EID: 0031993260     PISSN: 09671994     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0967199400005025     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0030447353 scopus 로고    scopus 로고
    • The primary structure and carbohydrate specificity of a β-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis
    • Ahmed, H., Pohl, J., Fink, N.E., Strobel, F. & Vasta, G.R. (1996). The primary structure and carbohydrate specificity of a β-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis. J. Biol. Chem. 271, 33 083-94.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33083-33094
    • Ahmed, H.1    Pohl, J.2    Fink, N.E.3    Strobel, F.4    Vasta, G.R.5
  • 2
    • 0026753050 scopus 로고
    • Changes in expression of the endogenous β-galactoside-binding 14-kDa lectin of chick embryonic skin during epidermal differentiation
    • Akimoto, Y., Kawakami, H., Oda, Y., Obinata, A., Endo, H., Kasai, K. & Hirano, H. (1992). Changes in expression of the endogenous β-galactoside-binding 14-kDa lectin of chick embryonic skin during epidermal differentiation. Exp. Cell Res. 199, 297-304.
    • (1992) Exp. Cell Res. , vol.199 , pp. 297-304
    • Akimoto, Y.1    Kawakami, H.2    Oda, Y.3    Obinata, A.4    Endo, H.5    Kasai, K.6    Hirano, H.7
  • 3
    • 0027197286 scopus 로고
    • Secretion of endogenous 16-kDa β-galactoside-binding lectin from vitamin A-pretreated chick embryonic cultured skin
    • Akimoto, Y., Obinata, A., Hirabayashi, J., Sakakura, Y., Endo, H., Kasai, K. & Hirano, H. (1993). Secretion of endogenous 16-kDa β-galactoside-binding lectin from vitamin A-pretreated chick embryonic cultured skin. Exp. Cell Res. 205, 251-60.
    • (1993) Exp. Cell Res. , vol.205 , pp. 251-260
    • Akimoto, Y.1    Obinata, A.2    Hirabayashi, J.3    Sakakura, Y.4    Endo, H.5    Kasai, K.6    Hirano, H.7
  • 4
    • 0028904333 scopus 로고
    • Expression of the endogenous 14-kDa β-galactoside-binding lectin galectin in normal human skin
    • Akimoto, Y., Hirabayashi, J., Kasai, K. & Hirano, H. (1995a). Expression of the endogenous 14-kDa β-galactoside-binding lectin galectin in normal human skin. Cell Tissue Res. 280, 1-10.
    • (1995) Cell Tissue Res. , vol.280 , pp. 1-10
    • Akimoto, Y.1    Hirabayashi, J.2    Kasai, K.3    Hirano, H.4
  • 5
    • 0028798759 scopus 로고
    • Changes in expression of two endogenous β-galactoside-binding isolectins in the dermis of chick embryonic skin during development in ovo and in vitro
    • Akimoto, Y., Obinata, A., Hirabayashi, J., Sakakura, Y., Endo, H., Kasai, K. & Hirano, H. (1995b). Changes in expression of two endogenous β-galactoside-binding isolectins in the dermis of chick embryonic skin during development in ovo and in vitro. Cell Tissue Res. 279, 3-12.
    • (1995) Cell Tissue Res. , vol.279 , pp. 3-12
    • Akimoto, Y.1    Obinata, A.2    Hirabayashi, J.3    Sakakura, Y.4    Endo, H.5    Kasai, K.6    Hirano, H.7
  • 7
    • 0022538256 scopus 로고
    • Characterization of yolk platelets isolated from developing embryos of Arbacia punctulata
    • Armant, D.R., Carson, D.D., Decker, G.L., Welply, J.K. & Lennarz, W.J. (1986). Characterization of yolk platelets isolated from developing embryos of Arbacia punctulata. Dev. Biol. 113, 342-55.
    • (1986) Dev. Biol. , vol.113 , pp. 342-355
    • Armant, D.R.1    Carson, D.D.2    Decker, G.L.3    Welply, J.K.4    Lennarz, W.J.5
  • 10
    • 0027965708 scopus 로고
    • Galectins: Structure and function of a large family of animal lectins
    • Barondes, S.H., Cooper, D.N.W., Gitt, M.A. & Leffler, H. (1994b). Galectins: structure and function of a large family of animal lectins. J. Biol. Chem. 269, 20 807-10.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.W.2    Gitt, M.A.3    Leffler, H.4
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-54.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0021246322 scopus 로고
    • Endogenous mammalian lectin localized extracellularly in lung elastic fibers
    • Cerra, R.F., Haywood-Reid, P.L. & Barondes, S.H. (1984). Endogenous mammalian lectin localized extracellularly in lung elastic fibers. J. Cell Biol. 98, 1580-9.
    • (1984) J. Cell Biol. , vol.98 , pp. 1580-1589
    • Cerra, R.F.1    Haywood-Reid, P.L.2    Barondes, S.H.3
  • 14
    • 0024587474 scopus 로고
    • Evidence for precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion
    • Cervello, M. & Matranga, V. (1989). Evidence for precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion. Cell Differ. Dev. 26, 67-76.
    • (1989) Cell Differ. Dev. , vol.26 , pp. 67-76
    • Cervello, M.1    Matranga, V.2
  • 15
    • 0028986607 scopus 로고
    • Galectin-1, a β-galactoside-binding lectin in Chinese hamster ovary cells
    • Cho, M. & Cummings, R.D. (1995). Galectin-1, a β-galactoside-binding lectin in Chinese hamster ovary cells. J. Biol. Chem. 270, 5207-12.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5207-5212
    • Cho, M.1    Cummings, R.D.2
  • 16
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper, D.N.W. & Barondes, S.H. (1990). Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J. Cell Biol. 110, 1681-91.
    • (1990) J. Cell Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 17
    • 0025786162 scopus 로고
    • Endogenous muscle lectin inhibits myoblast adhesion to laminin
    • Cooper, D.N.W., Massa, S.M. & Barondes, S.H. (1991). Endogenous muscle lectin inhibits myoblast adhesion to laminin. J. Cell Biol. 115, 1437-48.
    • (1991) J. Cell Biol. , vol.115 , pp. 1437-1448
    • Cooper, D.N.W.1    Massa, S.M.2    Barondes, S.H.3
  • 18
    • 0028855759 scopus 로고
    • Identificalion of galectin-3 as a factor in pre-mRNA splicing
    • Dagher, S.F., Wang, J.L. & Patterson, R.J. (1995). Identificalion of galectin-3 as a factor in pre-mRNA splicing. Proc. Natl. Acad. Sci. USA 92, 1213-17.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1213-1217
    • Dagher, S.F.1    Wang, J.L.2    Patterson, R.J.3
  • 19
    • 0001350949 scopus 로고
    • Serie tipo de los primeros estadios èmbrionarios en Bufo arenarum
    • Del Conte, E. & Sirlin, J.L. (1951). Serie tipo de los primeros estadios èmbrionarios en Bufo arenarum. Acta Zool. Lilloana 12, 495-9.
    • (1951) Acta Zool. Lilloana , vol.12 , pp. 495-499
    • Del Conte, E.1    Sirlin, J.L.2
  • 20
    • 0023904329 scopus 로고
    • Lectin activity and distribution of chicken lactose lectin I in the extracellular matrix of the chick developing kidney
    • Didier, E., Didier, P., Bayle, D. & Chevalier, M. (1988). Lectin activity and distribution of chicken lactose lectin I in the extracellular matrix of the chick developing kidney. Cell Differ. 24, 83-96.
    • (1988) Cell Differ. , vol.24 , pp. 83-96
    • Didier, E.1    Didier, P.2    Bayle, D.3    Chevalier, M.4
  • 21
    • 0029906113 scopus 로고    scopus 로고
    • Purification and partial biochemical characterization of an S-type lectin from blastula embryos of Bufo arenarum
    • Elola, M.T. & Fink, N.E. (1996). Purification and partial biochemical characterization of an S-type lectin from blastula embryos of Bufo arenarum. Cotnp. Biochem. Physiol. 115, 175-82.
    • (1996) Cotnp. Biochem. Physiol. , vol.115 , pp. 175-182
    • Elola, M.T.1    Fink, N.E.2
  • 24
    • 0023642594 scopus 로고
    • Purification and some characteristics of a β-galactoside binding soluble lectin from amphibian ovary
    • Fink de Cabutti, N.E., Caron, M., Joubert, R., Elola, M.T., Bladier, D. & Herkovits, J. (1987). Purification and some characteristics of a β-galactoside binding soluble lectin from amphibian ovary. FEBS Lett. 223, 330-4.
    • (1987) FEBS Lett. , vol.223 , pp. 330-334
    • Fink De Cabutti, N.E.1    Caron, M.2    Joubert, R.3    Elola, M.T.4    Bladier, D.5    Herkovits, J.6
  • 25
    • 0025560214 scopus 로고
    • An endogenous carbohydrate-binding protein of baby hamster kidney (BHK21 C13) cells
    • Foddy, L., Stamatoglou, S.C. & Hughes, R.C. (1990). An endogenous carbohydrate-binding protein of baby hamster kidney (BHK21 C13) cells. J. Cell Sci. 97, 139-48.
    • (1990) J. Cell Sci. , vol.97 , pp. 139-148
    • Foddy, L.1    Stamatoglou, S.C.2    Hughes, R.C.3
  • 26
    • 0028998657 scopus 로고
    • Galectin-3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo
    • Fowlis, D., Colnot, C., Ripoche, M.-A. & Poirier, F. (1995). Galectin-3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo. Dev. Dynam. 203, 241-51.
    • (1995) Dev. Dynam. , vol.203 , pp. 241-251
    • Fowlis, D.1    Colnot, C.2    Ripoche, M.-A.3    Poirier, F.4
  • 27
    • 0028053242 scopus 로고
    • 1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation
    • 1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation. J. Cell Sci. 107, 175-81.
    • (1994) J. Cell Sci. , vol.107 , pp. 175-181
    • Gu, M.1    Wang, W.2    Song, W.K.3    Cooper, D.N.W.4    Kaufman, S.J.5
  • 30
    • 0026519309 scopus 로고
    • The 14 kDa β-galactoside binding lectin in myoblast and myotubes cultures: Localization by confocal microscopy
    • Harrison, F.L. & Wilson, T.J.G. (1992). The 14 kDa β-galactoside binding lectin in myoblast and myotubes cultures: localization by confocal microscopy. J. Cell Sci. 101, 635-46.
    • (1992) J. Cell Sci. , vol.101 , pp. 635-646
    • Harrison, F.L.1    Wilson, T.J.G.2
  • 31
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi, J. & Kasai, K. (1993). The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3, 297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 32
    • 0024399009 scopus 로고
    • Are nuclear lectins and nuclear glycoproteins involved in the modulation of nuclear functions?
    • Hubert, J., Seve, A.P., Facy, P. & Monsigny, M. (1989). Are nuclear lectins and nuclear glycoproteins involved in the modulation of nuclear functions? Cell Differ. Dev. 27, 69-81.
    • (1989) Cell Differ. Dev. , vol.27 , pp. 69-81
    • Hubert, J.1    Seve, A.P.2    Facy, P.3    Monsigny, M.4
  • 33
    • 0029102299 scopus 로고
    • Functional evidence that cell surface galectin-3 mediates homotypic cell adhesion
    • Inohara, H. & Raz, A. (1995). Functional evidence that cell surface galectin-3 mediates homotypic cell adhesion. Cancer Res. 55, 3267-71.
    • (1995) Cancer Res. , vol.55 , pp. 3267-3271
    • Inohara, H.1    Raz, A.2
  • 35
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • Kasai, K. & Hirabayashi, J. (1996). Galectins: a family of animal lectins that decipher glycocodes. J. Biochem. 119, 1-8.
    • (1996) J. Biochem. , vol.119 , pp. 1-8
    • Kasai, K.1    Hirabayashi, J.2
  • 36
    • 0022394368 scopus 로고
    • Inhibition of tumor cell colony formation in culture by a monoclonal antibody to endogenous lectins
    • Lotan, R., Lotan, D. & Raz, A. (1985). Inhibition of tumor cell colony formation in culture by a monoclonal antibody to endogenous lectins. Cancer Res. 4,5, 4349-53.
    • (1985) Cancer Res. , vol.4-5 , pp. 4349-4353
    • Lotan, R.1    Lotan, D.2    Raz, A.3
  • 37
    • 0027414461 scopus 로고
    • Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma
    • Lotz, M.M., Andrews, C.W. Jr, Korzelius, C.A., Lee, E.C., Steele, G.D., Clarke, A. & Mercurio, A.M. (1993). Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma. Proc. Natl. Acad. Sci. USA 90, 3466-70.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3466-3470
    • Lotz, M.M.1    Andrews Jr., C.W.2    Korzelius, C.A.3    Lee, E.C.4    Steele, G.D.5    Clarke, A.6    Mercurio, A.M.7
  • 38
    • 0028229493 scopus 로고
    • Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism
    • Mahanthappa, N.K., Cooper, D.N.W., Barondes, S.H. & Schwarting, G.A. (1994). Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism. Development 120, 1373-84.
    • (1994) Development , vol.120 , pp. 1373-1384
    • Mahanthappa, N.K.1    Cooper, D.N.W.2    Barondes, S.H.3    Schwarting, G.A.4
  • 39
    • 0026627818 scopus 로고
    • Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin
    • Marschal, P., Herrmann, J., Leffler, H., Barondes, S.H. & Cooper, D.N.W. (1992). Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin. J. Biol. Chem. 267, 12 942-9.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12942-12949
    • Marschal, P.1    Herrmann, J.2    Leffler, H.3    Barondes, S.H.4    Cooper, D.N.W.5
  • 40
    • 0028304650 scopus 로고
    • Xenopus laevis L-14 lectin is expressed in a typical pattern in the adult, but is absent from embryonic tissues
    • Marschal, P., Cannon, V., Barondes, S.H. & Cooper, D.N.W. (1994). Xenopus laevis L-14 lectin is expressed in a typical pattern in the adult, but is absent from embryonic tissues. Glycobiology 4, 297-305.
    • (1994) Glycobiology , vol.4 , pp. 297-305
    • Marschal, P.1    Cannon, V.2    Barondes, S.H.3    Cooper, D.N.W.4
  • 41
    • 0022569861 scopus 로고
    • Endogenous lectins from cultured cells: Subcellular localization of carbohydrate-binding protein 35 in 3T3 fibroblasts
    • Moutsatsos, I.K., Davis, J.M. & Wang, J.L. (1986). Endogenous lectins from cultured cells: subcellular localization of carbohydrate-binding protein 35 in 3T3 fibroblasts. J. Cell Biol. 102, 477-83.
    • (1986) J. Cell Biol. , vol.102 , pp. 477-483
    • Moutsatsos, I.K.1    Davis, J.M.2    Wang, J.L.3
  • 42
    • 0023406938 scopus 로고
    • Endogenous lectins from cultured cells: Nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts
    • Moutsatsos, I.K., Wade, M., Schindler, M. & Wang, J.L. (1987). Endogenous lectins from cultured cells: nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA 84, 6452-6.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6452-6456
    • Moutsatsos, I.K.1    Wade, M.2    Schindler, M.3    Wang, J.L.4
  • 43
    • 0026504062 scopus 로고
    • The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus
    • Muramoto, K. & Kamiya, H. (1992). The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus. Biochim. Biophys. Acta 1116, 129-36.
    • (1992) Biochim. Biophys. Acta , vol.1116 , pp. 129-136
    • Muramoto, K.1    Kamiya, H.2
  • 44
    • 0027945617 scopus 로고
    • Concomitant increases in galectin-1 and its glycoconjugate ligands (carcinoembryonic antigen, Lamp-1, and Lamp-2) in cultured human colon carcinoma cells by sodium butyrate
    • Ohannesian, D.W., Lotan, D. & Lotan, R. (1994). Concomitant increases in galectin-1 and its glycoconjugate ligands (carcinoembryonic antigen, Lamp-1, and Lamp-2) in cultured human colon carcinoma cells by sodium butyrate. Cancer Res. 54, 5992-6000.
    • (1994) Cancer Res. , vol.54 , pp. 5992-6000
    • Ohannesian, D.W.1    Lotan, D.2    Lotan, R.3
  • 45
    • 0023686544 scopus 로고
    • Isolation and characterization of the chick 14K β-galactoside-binding lectin gene
    • Ohyama, Y. & Kasai, K. (1988). Isolation and characterization of the chick 14K β-galactoside-binding lectin gene. J. Biochem. 104, 173-7.
    • (1988) J. Biochem. , vol.104 , pp. 173-177
    • Ohyama, Y.1    Kasai, K.2
  • 46
    • 0025901028 scopus 로고
    • Purification and characterization of a β-galactoside binding lectin from frog (Rana catesbeiana) eggs
    • Ozeki, Y, Matsui, T., Nitta, K., Kawauchi, H., Takayanagi, Y. & Titani, K. (1991). Purification and characterization of a β-galactoside binding lectin from frog (Rana catesbeiana) eggs. Biochem. Biophys. Res. Commun. 178, 407-13.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 407-413
    • Ozeki, Y.1    Matsui, T.2    Nitta, K.3    Kawauchi, H.4    Takayanagi, Y.5    Titani, K.6
  • 48
    • 0026724472 scopus 로고
    • Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre- and post-implantation development
    • Poirier, F., Timmons, P.M., Chan, C.-T.J., Guénet, J.-L. & Rigby, P.W.J. (1992). Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre- and post-implantation development. Development 115, 143-55.
    • (1992) Development , vol.115 , pp. 143-155
    • Poirier, F.1    Timmons, P.M.2    Chan, C.-T.J.3    Guénet, J.-L.4    Rigby, P.W.J.5
  • 49
    • 0025642403 scopus 로고
    • Structure of chicken 16-kDa β-galactoside-binding lectin: Complete amino acid sequence, cloning of cDNA, and production of recombinant lectin
    • Sakakura, Y., Hirabayashi, J., Oda, Y., Ohyama, Y. & Kasai, K. (1990). Structure of chicken 16-kDa β-galactoside-binding lectin: complete amino acid sequence, cloning of cDNA, and production of recombinant lectin. J. Biol. Chem. 265, 21 573-9.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21573-21579
    • Sakakura, Y.1    Hirabayashi, J.2    Oda, Y.3    Ohyama, Y.4    Kasai, K.5
  • 50
    • 0024145678 scopus 로고
    • RNA metabolism in the follicle cells of Bufo arenarum oocytes. II. Autoradiographic studies
    • Sánchez Riera, A.M., Sánchez, S.S. & Cabada, M.O. (1988). RNA metabolism in the follicle cells of Bufo arenarum oocytes. II. Autoradiographic studies. Micr. Electr. Biol. Cell. 12, 163-76.
    • (1988) Micr. Electr. Biol. Cell. , vol.12 , pp. 163-176
    • Sánchez Riera, A.M.1    Sánchez, S.S.2    Cabada, M.O.3
  • 51
    • 0025639067 scopus 로고
    • The endogenous lectins of the chick blastoderm are present in association with an apolipoprotein in distinct organelles and in the extracellular matrix
    • Sanders, E.J., Zalik, S.E., Schneider, W.J. & Ledsham, Y.M. (1990). The endogenous lectins of the chick blastoderm are present in association with an apolipoprotein in distinct organelles and in the extracellular matrix. Rouxs Arch. Dev. Biol. 199, 295-306.
    • (1990) Rouxs Arch. Dev. Biol. , vol.199 , pp. 295-306
    • Sanders, E.J.1    Zalik, S.E.2    Schneider, W.J.3    Ledsham, Y.M.4
  • 52
    • 0028074969 scopus 로고
    • Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages
    • Sato, S. & Hughes, R.C. (1994). Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J. Biol. Chem. 269, 4424-30.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4424-4430
    • Sato, S.1    Hughes, R.C.2
  • 53
    • 0019256745 scopus 로고
    • Studies of oogenesis in Bufo arenarum
    • Valdez Toledo, C.L. & Pisanó, A. (1980). Studies of oogenesis in Bufo arenarum. Reproduction 4, 315-30.
    • (1980) Reproduction , vol.4 , pp. 315-330
    • Valdez Toledo, C.L.1    Pisanó, A.2
  • 54
    • 0026523484 scopus 로고
    • Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex
    • Wang, J.L., Werner, E.A., Laing, J.G. & Patterson, R.J. (1992). Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex. Biochem. Soc. Trans. 20, 269-74.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 269-274
    • Wang, J.L.1    Werner, E.A.2    Laing, J.G.3    Patterson, R.J.4
  • 55
    • 0025218968 scopus 로고
    • The gastrulating chick blastoderm contains 16 kDa and 14-kDa galactose-binding lectins possibly associated with an apolipoprotein
    • Zalik, S.E., Schneider, W.J. & Ledsham, I.M. (1990). The gastrulating chick blastoderm contains 16 kDa and 14-kDa galactose-binding lectins possibly associated with an apolipoprotein. Cell Differ. Dev. 29, 217-31.
    • (1990) Cell Differ. Dev. , vol.29 , pp. 217-231
    • Zalik, S.E.1    Schneider, W.J.2    Ledsham, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.