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Volumn 73, Issue 11, 2008, Pages 1060-1065

Fluorescence study of steroid hormone binding activity of Helix pomatia agglutinin

Author keywords

Adenine; Helix pomatia agglutinin; Progesterone; Steroid hormones; Testosterone; Trp fluorescence

Indexed keywords

ADENINE; AGGLUTININ; HELIX POMATIA AGGLUTININ; LECTIN; N ACETYLGALACTOSAMINE; PROGESTERONE; STEROID HORMONE; TESTOSTERONE;

EID: 46949106298     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2008.04.003     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0028906957 scopus 로고
    • Vitelline coat of Unio elongatulus: III. Glycan chain analysis of the 220- and 180-kD components by means of lectins
    • Focarelli R., Leotta F., Lampariello R., and Rosati F. Vitelline coat of Unio elongatulus: III. Glycan chain analysis of the 220- and 180-kD components by means of lectins. Mol Reprod Dev 40 (1995) 205-210
    • (1995) Mol Reprod Dev , vol.40 , pp. 205-210
    • Focarelli, R.1    Leotta, F.2    Lampariello, R.3    Rosati, F.4
  • 2
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: carbohydrate-specific reagents and biological recognition molecules
    • Sharon N. Lectins: carbohydrate-specific reagents and biological recognition molecules. J Biol Chem 282 (2007) 2753-2764
    • (2007) J Biol Chem , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 3
    • 0021015566 scopus 로고
    • Adenine binding sites of the lectin from lima beans (Phaseolus lunatus)
    • Roberts D.D., and Goldstein I.J. Adenine binding sites of the lectin from lima beans (Phaseolus lunatus). J Biol Chem 258 (1983) 13820-13824
    • (1983) J Biol Chem , vol.258 , pp. 13820-13824
    • Roberts, D.D.1    Goldstein, I.J.2
  • 4
    • 0025884394 scopus 로고
    • Crystallization and preliminary X-ray analysis of peanut agglutinin-N6-benzylaminopurine complex
    • Zaluzec E.J., Zaluzek M.M., Olsen K.W., and Pavkovic S.F. Crystallization and preliminary X-ray analysis of peanut agglutinin-N6-benzylaminopurine complex. J Mol Biol 219 (1991) 151-153
    • (1991) J Mol Biol , vol.219 , pp. 151-153
    • Zaluzec, E.J.1    Zaluzek, M.M.2    Olsen, K.W.3    Pavkovic, S.F.4
  • 5
    • 0026764816 scopus 로고
    • Characterization of the adenine binding sites of two Dolichos biflorus lectins
    • Gegg C.V., Roberts D.D., Segel I.H., and Etzler M.E. Characterization of the adenine binding sites of two Dolichos biflorus lectins. Biochemistry 31 (1992) 6938-6942
    • (1992) Biochemistry , vol.31 , pp. 6938-6942
    • Gegg, C.V.1    Roberts, D.D.2    Segel, I.H.3    Etzler, M.E.4
  • 6
    • 0033525658 scopus 로고    scopus 로고
    • Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus
    • Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.H., Strecker G., Imberty A., et al. Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus. J Mol Biol 286 (1999) 1161-1177
    • (1999) J Mol Biol , vol.286 , pp. 1161-1177
    • Hamelryck, T.W.1    Loris, R.2    Bouckaert, J.3    Dao-Thi, M.H.4    Strecker, G.5    Imberty, A.6
  • 8
    • 33644897618 scopus 로고    scopus 로고
    • Beyond carbohydrate binding: new directions in plant lectin research
    • Komath S.S., Kavitha M., and Swamy M.J. Beyond carbohydrate binding: new directions in plant lectin research. Org Biomol Chem 4 (2006) 973-988
    • (2006) Org Biomol Chem , vol.4 , pp. 973-988
    • Komath, S.S.1    Kavitha, M.2    Swamy, M.J.3
  • 9
    • 33750487493 scopus 로고    scopus 로고
    • Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachnis hypogaea) lectin SL-I
    • Pathak M., Singh B., Sharma A., Agrawal P., Pasha S., Das H.R., et al. Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachnis hypogaea) lectin SL-I. Plant Mol Biol 62 (2006) 529-545
    • (2006) Plant Mol Biol , vol.62 , pp. 529-545
    • Pathak, M.1    Singh, B.2    Sharma, A.3    Agrawal, P.4    Pasha, S.5    Das, H.R.6
  • 10
    • 0037454717 scopus 로고    scopus 로고
    • Binding of hydrophobic ligands by Pseudomonas aeruginosa PA-I lectin
    • Stoitsova S.R., Boteva R.N., and Doyle R.J. Binding of hydrophobic ligands by Pseudomonas aeruginosa PA-I lectin. Biochim Biophys Acta 1619 (2003) 213-219
    • (2003) Biochim Biophys Acta , vol.1619 , pp. 213-219
    • Stoitsova, S.R.1    Boteva, R.N.2    Doyle, R.J.3
  • 11
    • 13444271958 scopus 로고    scopus 로고
    • PA-I lectin from Pseudomonas aeruginosa binds acyl homoserine lactones
    • Boteva R., Bogoeva V., and Stoitsova S. PA-I lectin from Pseudomonas aeruginosa binds acyl homoserine lactones. Biochim Biophys Acta 1747 (2005) 143-149
    • (2005) Biochim Biophys Acta , vol.1747 , pp. 143-149
    • Boteva, R.1    Bogoeva, V.2    Stoitsova, S.3
  • 12
    • 0028178318 scopus 로고
    • Non-carbohydrate binding partners/domains of animal lectins
    • Gabius H.J. Non-carbohydrate binding partners/domains of animal lectins. Int J Biochem 26 (1994) 469-477
    • (1994) Int J Biochem , vol.26 , pp. 469-477
    • Gabius, H.J.1
  • 13
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: a historical introduction and overview
    • Kilpatrick D.C. Animal lectins: a historical introduction and overview. Biochim Biophys Acta 1572 (2002) 187-197
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 14
    • 0019380146 scopus 로고
    • Lectins: their multiple endogenous cellular functions
    • Barondes S.H. Lectins: their multiple endogenous cellular functions. Annu Rev Biochem 50 (1981) 207-231
    • (1981) Annu Rev Biochem , vol.50 , pp. 207-231
    • Barondes, S.H.1
  • 15
    • 0023938183 scopus 로고
    • The elastin receptor: a galactoside binding protein
    • Hinck A., Wrenn D.S., Mecham R.P., and Barondes S.H. The elastin receptor: a galactoside binding protein. Science 239 (1988) 1539-1541
    • (1988) Science , vol.239 , pp. 1539-1541
    • Hinck, A.1    Wrenn, D.S.2    Mecham, R.P.3    Barondes, S.H.4
  • 16
    • 0030963839 scopus 로고    scopus 로고
    • The C-type lectin domains of lecticans, a family of aggregating chondrotin sulphate proteoglycans, bind tenasein-R by protein-protein interactions independent of carbohydrate moiety
    • Asperbg A., Mura R., Bourdoulous S., Shimonaka M., Heinegard D., Schashner M., et al. The C-type lectin domains of lecticans, a family of aggregating chondrotin sulphate proteoglycans, bind tenasein-R by protein-protein interactions independent of carbohydrate moiety. Proc Natl Acad Sci USA 94 (1997) 10116-10121
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10116-10121
    • Asperbg, A.1    Mura, R.2    Bourdoulous, S.3    Shimonaka, M.4    Heinegard, D.5    Schashner, M.6
  • 17
    • 0031559905 scopus 로고    scopus 로고
    • A novel type of binding specificity to phospholipids for rat mannose-binding proteins isolated from serum and liver
    • Kuroki Y., Honma T., Chiba H., Sano H., Saitoh M., Ogasawara Y., et al. A novel type of binding specificity to phospholipids for rat mannose-binding proteins isolated from serum and liver. FEBS Lett 414 (1997) 387-392
    • (1997) FEBS Lett , vol.414 , pp. 387-392
    • Kuroki, Y.1    Honma, T.2    Chiba, H.3    Sano, H.4    Saitoh, M.5    Ogasawara, Y.6
  • 18
    • 33745972080 scopus 로고    scopus 로고
    • Biochemical and structural analysis of Helix pomatia agglutinin. A hexameric lectin with a novel fold
    • Sanchez J.F., Lescar J., Chazalet V., Audfray A., Gagnon J., Alvarez R., et al. Biochemical and structural analysis of Helix pomatia agglutinin. A hexameric lectin with a novel fold. J Biol Chem 281 (2006) 20171-20180
    • (2006) J Biol Chem , vol.281 , pp. 20171-20180
    • Sanchez, J.F.1    Lescar, J.2    Chazalet, V.3    Audfray, A.4    Gagnon, J.5    Alvarez, R.6
  • 19
    • 0014224175 scopus 로고
    • A new source of antibody-like substances having anti-blood group specificity. A discussion on the specificity of Helix agglutinins
    • Prokop O., Uhlenbruck G., and Kohler W. A new source of antibody-like substances having anti-blood group specificity. A discussion on the specificity of Helix agglutinins. Vox Sang 14 (1968) 321-333
    • (1968) Vox Sang , vol.14 , pp. 321-333
    • Prokop, O.1    Uhlenbruck, G.2    Kohler, W.3
  • 20
    • 0015581478 scopus 로고
    • Routine identification of group-C streptococci by means of an agglutinin (protectin) from the albumen gland of the edible snail, Helix pomatia
    • Kohler W., Prokop O., and Kuhnemund O. Routine identification of group-C streptococci by means of an agglutinin (protectin) from the albumen gland of the edible snail, Helix pomatia. J Med Microbiol 6 (1973) 127-130
    • (1973) J Med Microbiol , vol.6 , pp. 127-130
    • Kohler, W.1    Prokop, O.2    Kuhnemund, O.3
  • 21
    • 4744359093 scopus 로고    scopus 로고
    • Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
    • Vasta G.R., Ahmed H., and Odom E.W. Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Curr Opin Struct Biol 14 (2004) 617-630
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 617-630
    • Vasta, G.R.1    Ahmed, H.2    Odom, E.W.3
  • 22
    • 33646152115 scopus 로고    scopus 로고
    • Sexual dimorphism in esterified steroid levels in the gastropod Marisa cornuarietis: the effect of xenoandrogenic compounds
    • Lyssimachou J.G., Bachmann A., Oehlmann J., Schulte-Oehlmann U., and Porte C. Sexual dimorphism in esterified steroid levels in the gastropod Marisa cornuarietis: the effect of xenoandrogenic compounds. Steroids 71 (2006) 435-444
    • (2006) Steroids , vol.71 , pp. 435-444
    • Lyssimachou, J.G.1    Bachmann, A.2    Oehlmann, J.3    Schulte-Oehlmann, U.4    Porte, C.5
  • 23
    • 33847131564 scopus 로고    scopus 로고
    • Steroids in aquatic invertebrates
    • Lafont R., and Mathieu M. Steroids in aquatic invertebrates. Ecotoxicology 16 (2007) 109-130
    • (2007) Ecotoxicology , vol.16 , pp. 109-130
    • Lafont, R.1    Mathieu, M.2
  • 24
    • 0001199956 scopus 로고
    • Steroid synthesizing capacity of the dorsal body of Helix pomatia L. (Gastropodia)-an in vitro study
    • Krush B., Shoenmakers H.J.N., Voogt P.A., and Nolte A. Steroid synthesizing capacity of the dorsal body of Helix pomatia L. (Gastropodia)-an in vitro study. Comp Biochem Physiol 64B (1979) 101-104
    • (1979) Comp Biochem Physiol , vol.64 B , pp. 101-104
    • Krush, B.1    Shoenmakers, H.J.N.2    Voogt, P.A.3    Nolte, A.4
  • 26
    • 0018621681 scopus 로고
    • Effect of oestrogenic, androgenic and gestigenic hormones on the gamatogeneis (oogenesis and spermatogenesis) in the snail (Helix pomatia)
    • Casaba B., and Birbauer J. Effect of oestrogenic, androgenic and gestigenic hormones on the gamatogeneis (oogenesis and spermatogenesis) in the snail (Helix pomatia). Acta Biol Med Ger 38 (1979) 1145-1148
    • (1979) Acta Biol Med Ger , vol.38 , pp. 1145-1148
    • Casaba, B.1    Birbauer, J.2
  • 27
    • 33846922784 scopus 로고    scopus 로고
    • Correlation between levels of sex hormones (progesterone, testosterone, and estrogen) and ecophysiological-behavior stages in two species of desert snails (Sphincterochila zonata and Sphincterochila prophetarum) in the Northern Negev Desert
    • Alon G., Shore L.S., and Steinberger Y. Correlation between levels of sex hormones (progesterone, testosterone, and estrogen) and ecophysiological-behavior stages in two species of desert snails (Sphincterochila zonata and Sphincterochila prophetarum) in the Northern Negev Desert. Gen Comp Endocrinol 151 (2007) 122-127
    • (2007) Gen Comp Endocrinol , vol.151 , pp. 122-127
    • Alon, G.1    Shore, L.S.2    Steinberger, Y.3
  • 28
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysosyme by iodide ion
    • Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysosyme by iodide ion. Biochemistry 10 (1971) 3254-3263
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 29
    • 0002091096 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Forster Th. Intermolecular energy migration and fluorescence. Ann Phys 2 (1948) 55-59
    • (1948) Ann Phys , vol.2 , pp. 55-59
    • Forster, Th.1
  • 30
    • 21344433863 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties
    • Jameson D.M., and Mocz G. Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties. Methods Mol Biol 305 (2005) 301-322
    • (2005) Methods Mol Biol , vol.305 , pp. 301-322
    • Jameson, D.M.1    Mocz, G.2
  • 31
    • 0030586746 scopus 로고    scopus 로고
    • Catalyc mechanism of mitochondrial processing peptidase: fluorescence studies
    • Boteva R., and Slavato B. Catalyc mechanism of mitochondrial processing peptidase: fluorescence studies. Arch Biochem Biophys 332 (1996) 323-328
    • (1996) Arch Biochem Biophys , vol.332 , pp. 323-328
    • Boteva, R.1    Slavato, B.2
  • 33
    • 0014592780 scopus 로고
    • Intramolecular energy transfer in adrenocorticotropin
    • Eisinger J. Intramolecular energy transfer in adrenocorticotropin. Biochemistry 8 (1969) 3902-3908
    • (1969) Biochemistry , vol.8 , pp. 3902-3908
    • Eisinger, J.1
  • 34
    • 0015163780 scopus 로고
    • Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides
    • Steinberg I.Z. Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides. Ann Rev Biochem 40 (1971) 83-89
    • (1971) Ann Rev Biochem , vol.40 , pp. 83-89
    • Steinberg, I.Z.1
  • 35
    • 0021101411 scopus 로고
    • Thermodynamics of binding between saccharides and Helix pomatia A hemagglutinin
    • Yoshii H., and Ishiyama N. Thermodynamics of binding between saccharides and Helix pomatia A hemagglutinin. Biochim Biophys Acta 742 (1983) 235-242
    • (1983) Biochim Biophys Acta , vol.742 , pp. 235-242
    • Yoshii, H.1    Ishiyama, N.2
  • 36
    • 19944378443 scopus 로고    scopus 로고
    • Testosterone-fatty acid esterification: a unique target for the endocrine toxicity of tributyltin to gastropods
    • LeBlanc G.A., Gooding M.P., and Sternberg R.M. Testosterone-fatty acid esterification: a unique target for the endocrine toxicity of tributyltin to gastropods. Integr. Compar. Biol. 45 (2005) 81-87
    • (2005) Integr. Compar. Biol. , vol.45 , pp. 81-87
    • LeBlanc, G.A.1    Gooding, M.P.2    Sternberg, R.M.3


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