메뉴 건너뛰기




Volumn 71, Issue 5-6, 2010, Pages 648-657

Toxic isolectins from the mushroom Boletus venenatus

Author keywords

Boletaceae; Boletus venenatus; Diarrhea; Lectin; Lethal toxicity; Mushroom; Purification

Indexed keywords

ALPHA FETOPROTEIN; ASIALOFETUIN; ASIALOGLYCOPROTEIN; CARBOHYDRATE; GLYCOPROTEIN; LECTIN; MYCOTOXIN; PLANT LECTIN; FETUIN;

EID: 77949642609     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.12.003     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 0035793553 scopus 로고    scopus 로고
    • Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans
    • Arata Y., Hirabayashi J., and Kasai K. Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. J. Biol. Chem. 276 (2001) 3068-3077
    • (2001) J. Biol. Chem. , vol.276 , pp. 3068-3077
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 3
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein 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
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 5
    • 0028851766 scopus 로고
    • Lipid peroxidation induced by bolesatine, a toxin of Boletus satanas: implication in m5dC variation in Vero cells related to inhibition of cell growth
    • Ennamany R., Marzetto S., Saboureau D., and Creppy E.E. Lipid peroxidation induced by bolesatine, a toxin of Boletus satanas: implication in m5dC variation in Vero cells related to inhibition of cell growth. Cell Biol. Toxicol. 11 (1995) 347-354
    • (1995) Cell Biol. Toxicol. , vol.11 , pp. 347-354
    • Ennamany, R.1    Marzetto, S.2    Saboureau, D.3    Creppy, E.E.4
  • 8
    • 0022448179 scopus 로고
    • Highly sensitive determination of N-acetyl- and N-glycolylneuraminic acids in human serum and urine and rat serum by reversed-phase liquid chromatography with fluorescence detection
    • Hara S., Yamaguchi M., Takemori Y., Nakamura M., and Ohkura Y. Highly sensitive determination of N-acetyl- and N-glycolylneuraminic acids in human serum and urine and rat serum by reversed-phase liquid chromatography with fluorescence detection. J. Chromatogr. 377 (1986) 111-119
    • (1986) J. Chromatogr. , vol.377 , pp. 111-119
    • Hara, S.1    Yamaguchi, M.2    Takemori, Y.3    Nakamura, M.4    Ohkura, Y.5
  • 9
    • 0024411583 scopus 로고
    • Determination of mono-O-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography
    • Hara S., Yamaguchi M., Takemori Y., Furuhata K., Ogura H., and Nakamura M. Determination of mono-O-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography. Anal. Biochem. 179 (1989) 162-166
    • (1989) Anal. Biochem. , vol.179 , pp. 162-166
    • Hara, S.1    Yamaguchi, M.2    Takemori, Y.3    Furuhata, K.4    Ogura, H.5    Nakamura, M.6
  • 10
    • 0032486273 scopus 로고    scopus 로고
    • Novel galactose-binding proteins in Annelida. Characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris
    • Hirabayashi J., Dutta S.K., and Kasai K. Novel galactose-binding proteins in Annelida. Characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris. J. Biol. Chem. 273 (1998) 14450-14460
    • (1998) J. Biol. Chem. , vol.273 , pp. 14450-14460
    • Hirabayashi, J.1    Dutta, S.K.2    Kasai, K.3
  • 11
    • 0034714622 scopus 로고    scopus 로고
    • Reinforcement of frontal affinity chromatography for effective analysis of lectin-oligosaccharide interactions
    • Hirabayashi J., Arata Y., and Kasai K. Reinforcement of frontal affinity chromatography for effective analysis of lectin-oligosaccharide interactions. J. Chromatogr. A 890 (2000) 261-271
    • (2000) J. Chromatogr. A , vol.890 , pp. 261-271
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.3
  • 12
    • 84950017292 scopus 로고
    • Mushroom lectins
    • Kawagishi H. Mushroom lectins. Food Rev. Int. 11 (1995) 63-68
    • (1995) Food Rev. Int. , vol.11 , pp. 63-68
    • Kawagishi, H.1
  • 13
    • 0028008670 scopus 로고
    • Two lectins from the marine sponge Halichondria okadai; an N-acetyl-sugar-specific lectin (HOL-I) and an N-acetyllactosamine-specific lectin (HOL-II)
    • Kawagishi H., Yamawaki M., Isobe S., Usui T., Kimura A., and Chiba S. Two lectins from the marine sponge Halichondria okadai; an N-acetyl-sugar-specific lectin (HOL-I) and an N-acetyllactosamine-specific lectin (HOL-II). J. Biol. Chem. 269 (1994) 1375-1379
    • (1994) J. Biol. Chem. , vol.269 , pp. 1375-1379
    • Kawagishi, H.1    Yamawaki, M.2    Isobe, S.3    Usui, T.4    Kimura, A.5    Chiba, S.6
  • 14
    • 0028265801 scopus 로고
    • A sialic acid-binding lectin from the mushroom Hericium erinaceum
    • Kawagishi H., Mori H., Uno A., Kimura A., and Chiba S. A sialic acid-binding lectin from the mushroom Hericium erinaceum. FEBS Lett. 340 (1994) 56-58
    • (1994) FEBS Lett. , vol.340 , pp. 56-58
    • Kawagishi, H.1    Mori, H.2    Uno, A.3    Kimura, A.4    Chiba, S.5
  • 16
    • 0035808489 scopus 로고    scopus 로고
    • Purification and characterization of a lectin from the mushroom Mycoleptodonoides aitchisonii
    • Kawagishi H., Takagi J., Taira T., Murata T., and Usui T. Purification and characterization of a lectin from the mushroom Mycoleptodonoides aitchisonii. Phytochemistry 56 (2001) 53-58
    • (2001) Phytochemistry , vol.56 , pp. 53-58
    • Kawagishi, H.1    Takagi, J.2    Taira, T.3    Murata, T.4    Usui, T.5
  • 17
    • 11144234544 scopus 로고    scopus 로고
    • Purification, characterization and sugar-binding specificity of an N-glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites
    • Kobayashi Y., Kobayashi K., Umehara K., Dohra H., Murata T., Usui T., and Kawagishi H. Purification, characterization and sugar-binding specificity of an N-glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites. J. Biol. Chem. 279 (2004) 53048-53055
    • (2004) J. Biol. Chem. , vol.279 , pp. 53048-53055
    • Kobayashi, Y.1    Kobayashi, K.2    Umehara, K.3    Dohra, H.4    Murata, T.5    Usui, T.6    Kawagishi, H.7
  • 18
    • 9944257938 scopus 로고    scopus 로고
    • Analysis of the carbohydrate binding specificity of the mushroom Pleurotus ostreatus lectin by surface plasmon resonance
    • Kobayashi Y., Nakamura H., Sekiguchi T., Takanami R., Murata T., Usui T., and Kawagishi H. Analysis of the carbohydrate binding specificity of the mushroom Pleurotus ostreatus lectin by surface plasmon resonance. Anal. Biochem. 336 (2005) 87-93
    • (2005) Anal. Biochem. , vol.336 , pp. 87-93
    • Kobayashi, Y.1    Nakamura, H.2    Sekiguchi, T.3    Takanami, R.4    Murata, T.5    Usui, T.6    Kawagishi, H.7
  • 19
    • 0024350505 scopus 로고
    • Purification and some properties of bolesatine, a protein inhibiting in vitro protein synthesis, from the mushroom Boletus satanas Lenz (Boletaceae)
    • Kretz O., Creppy E.E., Boulanger Y., and Dirheimer G. Purification and some properties of bolesatine, a protein inhibiting in vitro protein synthesis, from the mushroom Boletus satanas Lenz (Boletaceae). Arch. Toxicol. Suppl. 13 (1989) 422-427
    • (1989) Arch. Toxicol. Suppl. , vol.13 , pp. 422-427
    • Kretz, O.1    Creppy, E.E.2    Boulanger, Y.3    Dirheimer, G.4
  • 20
    • 0025970605 scopus 로고
    • Disposition of the toxic protein, bolesatine, in rats: its resistance to proteolytic enzymes
    • Kretz O., Creppy E.E., and Dirheimer G. Disposition of the toxic protein, bolesatine, in rats: its resistance to proteolytic enzymes. Xenobiotica 21 (1991) 65-73
    • (1991) Xenobiotica , vol.21 , pp. 65-73
    • Kretz, O.1    Creppy, E.E.2    Dirheimer, G.3
  • 21
    • 0026619945 scopus 로고
    • Properties of bolesatine, a translational inhibitor from Boletus satanas Lenz. Amino-terminal sequence determination and inhibition of rat mitochondrial protein synthesis
    • Kretz, O., Reinbolt, J., Creppy, E. E., Dirheimer, G., 1992a. Properties of bolesatine, a translational inhibitor from Boletus satanas Lenz. Amino-terminal sequence determination and inhibition of rat mitochondrial protein synthesis. Toxicol. Lett. 64-65 Spec No., 763-766.
    • (1992) Toxicol. Lett , vol.64-65 , Issue.SPEC and 763-766
    • Kretz, O.1    Reinbolt, J.2    Creppy, E.E.3    Dirheimer, G.4
  • 22
    • 85056012109 scopus 로고
    • Inhibition of protein synthesis in liver and kidney of mice by bolesatine: mechanistic approaches to the mode of action at the molecular level
    • Kretz O., Barbieri L., Creppy E.E., and Dirheimer G. Inhibition of protein synthesis in liver and kidney of mice by bolesatine: mechanistic approaches to the mode of action at the molecular level. Toxicology 73 (1992) 297-304
    • (1992) Toxicology , vol.73 , pp. 297-304
    • Kretz, O.1    Barbieri, L.2    Creppy, E.E.3    Dirheimer, G.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 33947481529 scopus 로고
    • The structures of Basidiomycete metabolites illudin S and illudin M
    • McMorris T.C., and Anchel M. The structures of Basidiomycete metabolites illudin S and illudin M. J. Am. Chem. Soc. 85 (1963) 831-832
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 831-832
    • McMorris, T.C.1    Anchel, M.2
  • 27
    • 0001524478 scopus 로고
    • On the determination of cystine as cysteic acid
    • Moore S. On the determination of cystine as cysteic acid. J. Biol. Chem. 238 (1963) 235-237
    • (1963) J. Biol. Chem. , vol.238 , pp. 235-237
    • Moore, S.1
  • 28
    • 0001307909 scopus 로고
    • Isolation of lampterol, an antitumor substance from Lampteromyces japonicus
    • Nakanishi K., Tada M., Yamada Y., Ohashi M., Komatsu N., and Terakawa H. Isolation of lampterol, an antitumor substance from Lampteromyces japonicus. Nature 197 (1963) 292
    • (1963) Nature , vol.197 , pp. 292
    • Nakanishi, K.1    Tada, M.2    Yamada, Y.3    Ohashi, M.4    Komatsu, N.5    Terakawa, H.6
  • 31
    • 0023631780 scopus 로고
    • Studies on the toxic components of Rhodophyllus rhodopolius. I. The biological activities and screening of the toxic principles
    • Suzuki K., Une T., Fujimoto H., and Yamazaki M. Studies on the toxic components of Rhodophyllus rhodopolius. I. The biological activities and screening of the toxic principles. Yakuga. Zasshi 107 (1987) 971-977
    • (1987) Yakuga. Zasshi , vol.107 , pp. 971-977
    • Suzuki, K.1    Une, T.2    Fujimoto, H.3    Yamazaki, M.4
  • 32
    • 0023972043 scopus 로고
    • Studies on the toxic components of Rhodophyllus rhodopolius. II. Partial purification and properties of the hemolysin from Rhodophyllus rhodopolius: examination on the condition of the hemolysis
    • Suzuki K., Une T., Fujimoto H., and Yamazaki M. Studies on the toxic components of Rhodophyllus rhodopolius. II. Partial purification and properties of the hemolysin from Rhodophyllus rhodopolius: examination on the condition of the hemolysis. Yakuga. Zasshi 108 (1988) 221-225
    • (1988) Yakuga. Zasshi , vol.108 , pp. 221-225
    • Suzuki, K.1    Une, T.2    Fujimoto, H.3    Yamazaki, M.4
  • 33
    • 0025043591 scopus 로고
    • Purification and some properties of a hemolysin from the poisonous mushroom Rhodophyllus rhodopolius
    • Suzuki K., Une T., Yamazaki M., and Takeda T. Purification and some properties of a hemolysin from the poisonous mushroom Rhodophyllus rhodopolius. Toxicon 28 (1990) 1019-1028
    • (1990) Toxicon , vol.28 , pp. 1019-1028
    • Suzuki, K.1    Une, T.2    Yamazaki, M.3    Takeda, T.4
  • 34
    • 0038732546 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis and application of glycopolymers containing multivalent sialyloligosaccharides with a poly(l-glutamic acid) backbone for inhibition of infection by influenza viruses
    • Totani K., Kubota T., Kuroda T., Murata T., Hidari K., Suzuki T., Suzuki Y., Kobayashi K., Ashida H., Yamamoto K., and Usui T. Chemo-enzymatic synthesis and application of glycopolymers containing multivalent sialyloligosaccharides with a poly(l-glutamic acid) backbone for inhibition of infection by influenza viruses. Glycobiology 13 (2003) 315-316
    • (2003) Glycobiology , vol.13 , pp. 315-316
    • Totani, K.1    Kubota, T.2    Kuroda, T.3    Murata, T.4    Hidari, K.5    Suzuki, T.6    Suzuki, Y.7    Kobayashi, K.8    Ashida, H.9    Yamamoto, K.10    Usui, T.11
  • 35
    • 3542999236 scopus 로고    scopus 로고
    • Lectins from mushrooms
    • Wang H., Ng T.B., and Ooi V.E.C. Lectins from mushrooms. Mycol. Res. 102 8 (1998) 897-906
    • (1998) Mycol. Res. , vol.102 , Issue.8 , pp. 897-906
    • Wang, H.1    Ng, T.B.2    Ooi, V.E.C.3
  • 36
    • 0000268895 scopus 로고    scopus 로고
    • Two-mode analysis by high-performance liquid chromatography of p-aminobenzoic ethyl ester-derivatized monosaccharides
    • Yasuno S., Murata T., Kokubo K., and Kamei M. Two-mode analysis by high-performance liquid chromatography of p-aminobenzoic ethyl ester-derivatized monosaccharides. Biosci. Biotech. Biochem. 61 (1997) 1944-1946
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 1944-1946
    • Yasuno, S.1    Murata, T.2    Kokubo, K.3    Kamei, M.4
  • 37
    • 0034327346 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopolypeptides carrying - Neu5Ac-(2 → 3)-d-Gal-(1 → 3)-D-GalNAc, -d-Gal-(1 → 3)-d-GalNAc, and related compounds and analysis of their specific interactions with lectins
    • Zeng X., Nakaaki Y., Murata T., and Usui T. Chemoenzymatic synthesis of glycopolypeptides carrying - Neu5Ac-(2 → 3)-d-Gal-(1 → 3)-D-GalNAc, -d-Gal-(1 → 3)-d-GalNAc, and related compounds and analysis of their specific interactions with lectins. Arch. Biochem. Biophys. 383 (2000) 28-37
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 28-37
    • Zeng, X.1    Nakaaki, Y.2    Murata, T.3    Usui, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.