메뉴 건너뛰기




Volumn 42, Issue 5, 2003, Pages 525-532

Purification and structural characterization of lectins from the cnidarian Bunodeopsis antillienis

Author keywords

Agglutinins; Anemone; Cnidarian; Lectins

Indexed keywords

BUNODEOPSIS ANTILLIENIS AGGLUTININ A; BUNODEOPSIS ANTILLIENIS AGGLUTININ B; CARBOHYDRATE; FUCOSE; GALACTOSE; GUANINE NUCLEOTIDE BINDING PROTEIN; LECTIN; MANNOSE; N ACETYLGALACTOSAMINE; PHOSPHATASE; PHOSPHOLIPASE A2; UNCLASSIFIED DRUG; AGGLUTININ A; AGGLUTININ B; AGGLUTININ-A; AGGLUTININ-B; HEMAGGLUTININ;

EID: 1542391746     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(03)00231-9     Document Type: Article
Times cited : (7)

References (21)
  • 1
    • 0034782028 scopus 로고    scopus 로고
    • Characterization of a bioactive 15 kDa fragment produced by proteolytic cleavage of chicken growth hormone
    • Arámburo C., Carranza M., Reyes M., Luna M., Martínez- Coria H., Berúmen L., Scanes C.G. Characterization of a bioactive 15 kDa fragment produced by proteolytic cleavage of chicken growth hormone. Endocrine. 15:2001;231-240.
    • (2001) Endocrine , vol.15 , pp. 231-240
    • Arámburo, C.1    Carranza, M.2    Reyes, M.3    Luna, M.4    Martínez-Coria, H.5    Berúmen, L.6    Scanes, C.G.7
  • 2
    • 0034703104 scopus 로고    scopus 로고
    • Lectins from tropical sponges
    • Bonay P.M., Fresno M. Lectins from tropical sponges. J. Biol. Chem. 275:2000;29283-29289.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29283-29289
    • Bonay, P.M.1    Fresno, M.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray H., Daecourt D., Strecker G., Spik G., Montruil J. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur. J. Biochem. 117:1981;41-55.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 41-55
    • Debray, H.1    Daecourt, D.2    Strecker, G.3    Spik, G.4    Montruil, J.5
  • 6
    • 0030579202 scopus 로고    scopus 로고
    • The role of localized cell surface-associated glycoproteins during fertilization in the hydrozoan Aequorea
    • Freeman G. The role of localized cell surface-associated glycoproteins during fertilization in the hydrozoan Aequorea. Dev. Biol. 179:1996;17-26.
    • (1996) Dev. Biol. , vol.179 , pp. 17-26
    • Freeman, G.1
  • 7
    • 0028501036 scopus 로고
    • Cell adhesion receptors and nuclear receptors are highly conserved from the lowest metazoa (marine sponges) to vertebrates
    • Gamlin V., Rinkevich B., Schake H., Kruse M., Muller I.M., Muller W.E.G. Cell adhesion receptors and nuclear receptors are highly conserved from the lowest metazoa (marine sponges) to vertebrates. Biol. Chem. Hoppe-Seyler. 375:1994;583-588.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 583-588
    • Gamlin, V.1    Rinkevich, B.2    Schake, H.3    Kruse, M.4    Muller, I.M.5    Muller, W.E.G.6
  • 8
    • 0033486238 scopus 로고    scopus 로고
    • 2 and co-lytic factor from sea anemone (Aiptasia pallida) nematocyst venom
    • 2 and co-lytic factor from sea anemone (Aiptasia pallida) nematocyst venom. Toxicon. 37:1999;1779-1796.
    • (1999) Toxicon , vol.37 , pp. 1779-1796
    • Grotendorst, G.R.1    Hessinger, D.A.2
  • 9
    • 0033961566 scopus 로고    scopus 로고
    • 2 component of sea anemone (Aiptasia pallida) nematocyst venom
    • 2 component of sea anemone (Aiptasia pallida) nematocyst venom. Toxicon. 38:2000;931-943.
    • (2000) Toxicon , vol.38 , pp. 931-943
    • Grotendorst, G.R.1    Hessenger, D.A.2
  • 10
    • 0032253972 scopus 로고
    • Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: Strategies and applications
    • Jensen O.N., Larsen M.R., Roepstorff P. Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: strategies and applications. Proteins Struct. Funct. Genet. Suppl. 999:1988;74-89.
    • (1988) Proteins Struct. Funct. Genet. Suppl. , vol.999 , pp. 74-89
    • Jensen, O.N.1    Larsen, M.R.2    Roepstorff, P.3
  • 11
    • 0034015805 scopus 로고    scopus 로고
    • The D-galactose-binding lectin of the octocoral Sinularia lochmodes: Characterization and possible relationship to the symbiotic dinoflagellates
    • Jimbo M., Yanohara T., Koike K., Koike K., Sakari R., Muramoto K., Kamiya H. The D-galactose-binding lectin of the octocoral Sinularia lochmodes: characterization and possible relationship to the symbiotic dinoflagellates. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 125:2000;227-236.
    • (2000) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.125 , pp. 227-236
    • Jimbo, M.1    Yanohara, T.2    Koike, K.3    Koike, K.4    Sakari, R.5    Muramoto, K.6    Kamiya, H.7
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-683.
    • (1970) Nature , vol.227 , pp. 680-683
    • Laemmli, U.K.1
  • 14
    • 0028972514 scopus 로고
    • 2+ influx, phosphoinositide hydrolysis, and histamine release induced by lysophosphatidylserine in mast cells
    • 2+ influx, phosphoinositide hydrolysis, and histamine release induced by lysophosphatidylserine in mast cells. J. Cell Physiol. 165:1995;89-95.
    • (1995) J. Cell Physiol. , vol.165 , pp. 89-95
    • Lloret, S.1    Moreno, J.J.2
  • 19
    • 0033732562 scopus 로고    scopus 로고
    • What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2?
    • Valentin E., Lambeau G. What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2? Biochimie. 82:2000;815-831.
    • (2000) Biochimie , vol.82 , pp. 815-831
    • Valentin, E.1    Lambeau, G.2
  • 20
    • 0024297848 scopus 로고
    • Purification and partial characterization of two lectins from the cactus Machaerocereus eruca
    • Zenteno E., Debray H., Montreuil J. Purification and partial characterization of two lectins from the cactus Machaerocereus eruca. FEBS Lett. 238:1988;95-100.
    • (1988) FEBS Lett. , vol.238 , pp. 95-100
    • Zenteno, E.1    Debray, H.2    Montreuil, J.3
  • 21
    • 0033066157 scopus 로고    scopus 로고
    • Lysis via the lectin pathway of complement activation: Minireview and lectin pathway enhancement of endotoxin-initiated hemolysis
    • Zhang Y., Suankratay C., Zhang X.-H., Lint T.F., Gewurz H. Lysis via the lectin pathway of complement activation: minireview and lectin pathway enhancement of endotoxin-initiated hemolysis. Immunopharmacology. 42:1999;81-90.
    • (1999) Immunopharmacology , vol.42 , pp. 81-90
    • Zhang, Y.1    Suankratay, C.2    Zhang, X.-H.3    Lint, T.F.4    Gewurz, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.