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Volumn 94, Issue 3-4, 2003, Pages 105-112

The immunostimulatory activity and stability of grass carp (Ctenopharyngodon idellus) roe lectin

Author keywords

Grass carp; Lectin; Rhamnose binding

Indexed keywords

ACID; ALKALI; LECTIN; SODIUM HYDROXIDE;

EID: 0142029184     PISSN: 01652427     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-2427(03)00067-9     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell G., Harford J. Carbohydrate-specific receptors of the liver. Annu. Rev. Biochem. 51:1982;531-534.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 531-534
    • Ashwell, G.1    Harford, J.2
  • 2
    • 0035802281 scopus 로고    scopus 로고
    • A serum fucolectin isolated and characterized from sea bass Dicentrarchus albrax
    • Cammarata M., Vazzana M., Chinnici C., Parrinello N. A serum fucolectin isolated and characterized from sea bass Dicentrarchus albrax. Biochim Biophys. Acta. 1528:2001;196-202.
    • (2001) Biochim Biophys. Acta. , vol.1528 , pp. 196-202
    • Cammarata, M.1    Vazzana, M.2    Chinnici, C.3    Parrinello, N.4
  • 5
    • 0032729109 scopus 로고    scopus 로고
    • Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. Biochim. Biophys
    • Hosono M., Ishikawa K., Mineki R., Murayama K., Numata C., Ogawa Y., Takayanagi Y., Nitta K. Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. Biochim. Biophys. Acta. 1472:1999;668-675.
    • (1999) Acta. , vol.1472 , pp. 668-675
    • Hosono, M.1    Ishikawa, K.2    Mineki, R.3    Murayama, K.4    Numata, C.5    Ogawa, Y.6    Takayanagi, Y.7    Nitta, K.8
  • 6
    • 0019556049 scopus 로고
    • Studies of O-glycosidically linked carbohydrate units of herring egg sialoglycoprotein
    • Iwasaki M., Inoue S. Studies of O-glycosidically linked carbohydrate units of herring egg sialoglycoprotein. J. Biochem. 2:1985;1067-1074.
    • (1985) J. Biochem. , vol.2 , pp. 1067-1074
    • Iwasaki, M.1    Inoue, S.2
  • 7
    • 85030965315 scopus 로고    scopus 로고
    • Krajhanzl, A., Danisova, A., Kocourek, J., Pancoska, P., 1985. In: Bog-Hansen, T.C., Spengler, G.A. (Eds.), Lectins - Biology, Biochemistry and Clinical Biochemistry, vol. 4. de Gruyter, Berlin, pp. 397-408.
    • Krajhanzl, A., Danisova, A., Kocourek, J., Pancoska, P., 1985. In: Bog-Hansen, T.C., Spengler, G.A. (Eds.), Lectins - Biology, Biochemistry and Clinical Biochemistry, vol. 4. de Gruyter, Berlin, pp. 397-408.
  • 8
    • 0024558286 scopus 로고
    • Bacterial action of fertilization envelope extract from eggs of the fish Cyprinus carpio and Plecoglossus altivelis
    • Kudo S., Inoue M. Bacterial action of fertilization envelope extract from eggs of the fish Cyprinus carpio and Plecoglossus altivelis. J. Exp. Zool. 250:1989;219-228.
    • (1989) J. Exp. Zool. , vol.250 , pp. 219-228
    • Kudo, S.1    Inoue, M.2
  • 10
    • 0036910590 scopus 로고    scopus 로고
    • Lam, Y.W., Ng, T.B., 2002. Purification and characterization of a rhamnose-binding lectin from grass carp (Ctenopharyngodon idellus) ovaries. Protein Expres. Purif. 26, 378-385.
    • Lam, Y.W., Ng, T.B., 2002. Purification and characterization of a rhamnose-binding lectin from grass carp (Ctenopharyngodon idellus) ovaries. Protein Expres. Purif. 26, 378-385.
  • 11
    • 0032501473 scopus 로고    scopus 로고
    • Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum
    • Lam S.S.L., Wang H.X., Ng T.B. Purification and characterization of novel ribosome inactivating proteins, alpha- and beta-pisavins, alpha- and beta-pisavins, from seeds of the garden pea Pisum sativum. Biochem. Biophys. Res. Co. 253:1998;135-142.
    • (1998) Biochem. Biophys. Res. Co. , vol.253 , pp. 135-142
    • Lam, S.S.L.1    Wang, H.X.2    Ng, T.B.3
  • 12
    • 0019876978 scopus 로고
    • Isolation and physicochemical characterization of electrolectin, a beta-D-galactoside binding lectin from the electric organ of Electrophorus electricus
    • Levi G., Teichberg V.I. Isolation and physicochemical characterization of electrolectin, a beta-D-galactoside binding lectin from the electric organ of Electrophorus electricus. J. Biol. Chem. 256:1981;5735-5740.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5735-5740
    • Levi, G.1    Teichberg, V.I.2
  • 13
    • 85030955643 scopus 로고    scopus 로고
    • Licastro, F., Barbieri, L., Krajhanzl, A., Kocourek, J., Stirpe, F., 1983. Effect of 32 purified animal and plant lectins on human T lymphocytes. In: Bog-Hansen, T.C., Spengler, G.A. (Eds.), Lectins - Biology, Biochemistry and Clinical Biochemistry. vol. 3. de Gruyter, Berlin, pp. 293-302.
    • Licastro, F., Barbieri, L., Krajhanzl, A., Kocourek, J., Stirpe, F., 1983. Effect of 32 purified animal and plant lectins on human T lymphocytes. In: Bog-Hansen, T.C., Spengler, G.A. (Eds.), Lectins - Biology, Biochemistry and Clinical Biochemistry. vol. 3. de Gruyter, Berlin, pp. 293-302.
  • 14
    • 0025961335 scopus 로고
    • A cortical lectin from the oocytes of Rutilus rutilus mitogenic activity and inhibition of protein synthesis
    • Licastro F., Barbieri L., Krajhanzl A., Kocourek J., Stirpe F. A cortical lectin from the oocytes of Rutilus rutilus mitogenic activity and inhibition of protein synthesis. Int. J. Biochem. 23:1991;101-105.
    • (1991) Int. J. Biochem. , vol.23 , pp. 101-105
    • Licastro, F.1    Barbieri, L.2    Krajhanzl, A.3    Kocourek, J.4    Stirpe, F.5
  • 15
    • 0025167425 scopus 로고
    • Isolation and characterization of a new lectin from plasma of fish Channa punctatus
    • Manihar S.R., Das H.R. Isolation and characterization of a new lectin from plasma of fish Channa punctatus. Biochim. Biophys. Acta. 1036:1990;162-165.
    • (1990) Biochim. Biophys. Acta , vol.1036 , pp. 162-165
    • Manihar, S.R.1    Das, H.R.2
  • 16
    • 0019876887 scopus 로고
    • Isolation and characterization of a mannan-binding protein from rat liver
    • Mizuno Y., Kozutsumi Y., Kawasaki T., Yamashina I. Isolation and characterization of a mannan-binding protein from rat liver. J. Biol. Chem. 256:1981;4247.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4247
    • Mizuno, Y.1    Kozutsumi, Y.2    Kawasaki, T.3    Yamashina, I.4
  • 17
    • 0030249213 scopus 로고    scopus 로고
    • Evidence that cortisol may protect against the immediate effects of stress on circulating leukocytes in the rainbow trout
    • Narnaware Y.K., Baker B.I. Evidence that cortisol may protect against the immediate effects of stress on circulating leukocytes in the rainbow trout. Gen. Comp. Endocr. 103:1996;359-366.
    • (1996) Gen. Comp. Endocr. , vol.103 , pp. 359-366
    • Narnaware, Y.K.1    Baker, B.I.2
  • 18
    • 51249168358 scopus 로고
    • The effects of various stresses, corticosteroids and adrenergic agents on phagocytosis in the rainbow trout
    • Narnaware Y.K., Baker B.I., Tomlinson M. The effects of various stresses, corticosteroids and adrenergic agents on phagocytosis in the rainbow trout. Fish Physiol. Biochem. 13:1994;131-140.
    • (1994) Fish Physiol. Biochem. , vol.13 , pp. 131-140
    • Narnaware, Y.K.1    Baker, B.I.2    Tomlinson, M.3
  • 19
    • 0031256526 scopus 로고    scopus 로고
    • Effect of injected growth hormone on phagocytosis of silver seabream (Sparus sarba) adapted to hyper- and hypo-osmotic salinities
    • Narnaware Y.K., Kelly S.P., Woo N.Y.S. Effect of injected growth hormone on phagocytosis of silver seabream (Sparus sarba) adapted to hyper- and hypo-osmotic salinities. Fish Shellfish Immun. 7:1997;515-517.
    • (1997) Fish Shellfish Immun. , vol.7 , pp. 515-517
    • Narnaware, Y.K.1    Kelly, S.P.2    Woo, N.Y.S.3
  • 20
    • 0032570905 scopus 로고    scopus 로고
    • Stimulation of macrophage phagocytosis and lymphocyte count by prolactin administration in silver seabream (Sparus sarba) adapted to hyper- and hypo-osmotic salinities
    • Narnaware Y.K., Kelly S.P., Woo N.Y.S. Stimulation of macrophage phagocytosis and lymphocyte count by prolactin administration in silver seabream (Sparus sarba) adapted to hyper- and hypo-osmotic salinities. Vet. Immunol. Immunopathol. 61:1998;387-391.
    • (1998) Vet. Immunol. Immunopathol. , vol.61 , pp. 387-391
    • Narnaware, Y.K.1    Kelly, S.P.2    Woo, N.Y.S.3
  • 21
    • 0021035829 scopus 로고
    • Studies on lectins LVII. Immunofluorescence localization of lectins present in fish ovaries
    • Nosek J., Krajhanzl A., Kocourek J. Studies on lectins LVII. Immunofluorescence localization of lectins present in fish ovaries. Histochemistry. 79:1984;131-139.
    • (1984) Histochemistry , vol.79 , pp. 131-139
    • Nosek, J.1    Krajhanzl, A.2    Kocourek, J.3
  • 22
    • 0021184457 scopus 로고
    • Purification and characterization of a fish lectin from the external mucus of Ophidiidae, Genypterus blacodes
    • Oda Y., Ichida S., Mimura T., Maeda K., Tsujikawa K., Aonuma S. Purification and characterization of a fish lectin from the external mucus of Ophidiidae, Genypterus blacodes. J. Pharmacobio-dyn. 7:1984;614-623.
    • (1984) J. Pharmacobio-dyn. , vol.7 , pp. 614-623
    • Oda, Y.1    Ichida, S.2    Mimura, T.3    Maeda, K.4    Tsujikawa, K.5    Aonuma, S.6
  • 23
    • 84969042365 scopus 로고
    • Induction of release of cytotoxin from murine bone marrow cells by an animal lectin
    • Okutomi T., Nakajima Y., Sakakibar F., Kawauchi H., Yamazaki M. Induction of release of cytotoxin from murine bone marrow cells by an animal lectin. Cancer Res. 47:1987;47-50.
    • (1987) Cancer Res. , vol.47 , pp. 47-50
    • Okutomi, T.1    Nakajima, Y.2    Sakakibar, F.3    Kawauchi, H.4    Yamazaki, M.5
  • 24
    • 0029841030 scopus 로고    scopus 로고
    • In vitro activation of fish phagocytic cells by growth hormone, prolaction and somatolactin
    • Sakai M., Kobayashi M., Kawauchi H. In vitro activation of fish phagocytic cells by growth hormone, prolaction and somatolactin. J. Endocrinol. 151:1996a;113-118.
    • (1996) J. Endocrinol. , vol.151 , pp. 113-118
    • Sakai, M.1    Kobayashi, M.2    Kawauchi, H.3
  • 25
    • 0030245903 scopus 로고    scopus 로고
    • Mitogenic effect of growth hormone and prolactin on chum salmon Oncorhynchus keta leucocytes in vitro
    • Sakai M., Kobayashi M., Kawauchi H. Mitogenic effect of growth hormone and prolactin on chum salmon Oncorhynchus keta leucocytes in vitro. Vet. Immunol. Immunopathol. 53:1996;185-189.
    • (1996) Vet. Immunol. Immunopathol. , vol.53 , pp. 185-189
    • Sakai, M.1    Kobayashi, M.2    Kawauchi, H.3
  • 26
    • 0021739921 scopus 로고
    • Phosphomannosyl receptor may participate in the adhesive interaction between lymphocytes and high endothelial venules
    • Stoolman J.M., Tenforde T.S., Roser R.D. Phosphomannosyl receptor may participate in the adhesive interaction between lymphocytes and high endothelial venules. J. Cell Biol. 99:1984;1535-1540.
    • (1984) J. Cell Biol. , vol.99 , pp. 1535-1540
    • Stoolman, J.M.1    Tenforde, T.S.2    Roser, R.D.3
  • 27
    • 0032563094 scopus 로고    scopus 로고
    • Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily
    • Tateno H., Saneyoshi A., Ogawa T., Muramoto K., Kamiya H., Saneyoshi M. Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily. J. Biol. Chem. 273:1998;19190-19197.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19190-19197
    • Tateno, H.1    Saneyoshi, A.2    Ogawa, T.3    Muramoto, K.4    Kamiya, H.5    Saneyoshi, M.6
  • 28
    • 0035376242 scopus 로고    scopus 로고
    • A novel rhamnose-binding lectin family from eggs of steelhead trout (Oncorhynchus mykiss) with different structures and tissue distribution
    • Tateno H., Ogawa T., Muramoto K., Kamiya H., Hirai T., Saneyoshi M. A novel rhamnose-binding lectin family from eggs of steelhead trout (Oncorhynchus mykiss) with different structures and tissue distribution. Biosci. Biotechnol. Biochem. 65:2001;1328-1338.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 1328-1338
    • Tateno, H.1    Ogawa, T.2    Muramoto, K.3    Kamiya, H.4    Hirai, T.5    Saneyoshi, M.6
  • 29
    • 0041289900 scopus 로고
    • β-D-Galactoside binding protein from electric organ tissue of Electrophorus electricus
    • Teichberg V.I., Silma I., Beitsch D.D., Resheff G. β-D-Galactoside binding protein from electric organ tissue of Electrophorus electricus. Proc. Natl. Acad. Sci. USA. 72:1975;1383-1387.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1383-1387
    • Teichberg, V.I.1    Silma, I.2    Beitsch, D.D.3    Resheff, G.4
  • 30
    • 84995198068 scopus 로고
    • Incomplete antibodies: A membrane problem
    • Uhlenbruck G., Prokop O. Incomplete antibodies: a membrane problem. Vox Sang. 12:1967;465-466.
    • (1967) Vox Sang. , vol.12 , pp. 465-466
    • Uhlenbruck, G.1    Prokop, O.2
  • 31
    • 0022982173 scopus 로고
    • Galactosyl-binding lectins from the tunicate Didemnum candidum. Purification and physicochemical characterization
    • Vasta G.R., Hunt J.C., Marchalonis J.J., Fish W.W. Galactosyl-binding lectins from the tunicate Didemnum candidum. Purification and physicochemical characterization. J. Biol. Chem. 261:1986;9174-9181.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9174-9181
    • Vasta, G.R.1    Hunt, J.C.2    Marchalonis, J.J.3    Fish, W.W.4
  • 32
    • 0028848256 scopus 로고
    • Isolation and characterization of two distinct lectins with antiproliferative activity from the mycelium of the edible mushroom Tricholoma mongolicum
    • Wang H.X., Ng T.B., Liu W.K., Ooi V.E.C., Chang S.T. Isolation and characterization of two distinct lectins with antiproliferative activity from the mycelium of the edible mushroom Tricholoma mongolicum. Int. J. Pept. Prot. Res. 46:1995;508-513.
    • (1995) Int. J. Pept. Prot. Res. , vol.46 , pp. 508-513
    • Wang, H.X.1    Ng, T.B.2    Liu, W.K.3    Ooi, V.E.C.4    Chang, S.T.5
  • 33
    • 0034692872 scopus 로고    scopus 로고
    • First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation
    • Wang H.X., Ye X., Ng T.B. First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation. Life Sci. 67:2000;2745-2752.
    • (2000) Life Sci. , vol.67 , pp. 2745-2752
    • Wang, H.X.1    Ye, X.2    Ng, T.B.3
  • 34
    • 0034618594 scopus 로고    scopus 로고
    • A new lectin with highly potent antihepatoma and antisarcoma activities from the oyster mushroom Pleurotus ostreatus
    • Wang H.X., Gao J., Ng T.B. A new lectin with highly potent antihepatoma and antisarcoma activities from the oyster mushroom Pleurotus ostreatus. Biochem. Biophys. Res. Co. 275:2001;810-816.
    • (2001) Biochem. Biophys. Res. Co. , vol.275 , pp. 810-816
    • Wang, H.X.1    Gao, J.2    Ng, T.B.3
  • 35
    • 0034912868 scopus 로고    scopus 로고
    • Purification of chrysancorin, a novel antifungal protein with mitogenic activity from garland chrysanthemum seeds
    • Wang H.X., Ye X.Y., Ng T.B. Purification of chrysancorin, a novel antifungal protein with mitogenic activity from garland chrysanthemum seeds. Biol. Chem. 382:2001;947-951.
    • (2001) Biol. Chem. , vol.382 , pp. 947-951
    • Wang, H.X.1    Ye, X.Y.2    Ng, T.B.3


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