메뉴 건너뛰기




Volumn 62, Issue 6, 1998, Pages 1211-1215

Structural analysis of n-linked carbohydrate chains of funnel web spider (agelenopsis aperta) venom peptide isomerase

Author keywords

N glycan; Peptide isomerase; Trimannosyl core structure; Two dimensional HPLC mapping; 1,6 fucosylation

Indexed keywords

2 AMINOPYRIDINE; ALPHA-AMINOPYRIDINE; AMINOPYRIDINE DERIVATIVE; FTX, SPIDER TOXIN; ISOMERASE; POLYAMINE; SPIDER VENOM;

EID: 0032087114     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1211     Document Type: Article
Times cited : (6)

References (22)
  • 1
    • 0024581791 scopus 로고
    • Deltorphin, a novel amphibian skin peptide with high selectivity and affinity for s opioid receptors
    • Kreil, G., Barra, D., Simmaco, M., Erspamer, V., Falconieri-E. G., Negri, L., Severini, C., and Cor si, R., Melchiorri, P., Deltorphin, a novel amphibian skin peptide with high selectivity and affinity for S opioid receptors. Eur. J. Pharmacol, 162, 123-128 (1989).
    • (1989) Eur. J. Pharmacol , vol.162 , pp. 123-128
    • Kreil, G.1    Barra, D.2    Simmaco, M.3    Erspamer, V.4
  • 2
    • 0028240333 scopus 로고
    • Peptides containing a d-amino acid from frogs and molluscs
    • Kreil, G., Peptides containing a D-amino acid from frogs and molluscs. J. Biol. Chem., 269, 10967-10970 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 10967-10970
    • Kreil, G.1
  • 3
    • 0028171637 scopus 로고
    • Co-agatoxin-tk containing d-serine at position 46, but not synthetic co-fl-ser46] agatoxin-tk, exerts blockade of p-type calcium channels in cerebellar purkinje neurons
    • Kuwada, M., Teramoto, T., Kumagaye, K. Y., Nakajima, K., Watanabe, T., Kawai, T., Kawakami, Y., Niidome, T., Sawada, K., Nishizawa, Y., and Katayama, K., co-Agatoxin-TK containing D-serine at position 46, but not synthetic co-fL-Ser46] agatoxin-TK, exerts blockade of P-type calcium channels in cerebellar Purkinje neurons. Mol Pharmacol, 46, 587-593 (1994).
    • (1994) Mol Pharmacol , vol.46 , pp. 587-593
    • Kuwada, M.1    Teramoto, T.2    Kumagaye, K.Y.3    Nakajima, K.4    Watanabe, T.5    Kawai, T.6    Kawakami, Y.7    Niidome, T.8    Sawada, K.9    Nishizawa, Y.10    Katayama, K.11
  • 4
    • 0028045629 scopus 로고
    • Disulfide bond assignment of co-agatoxins ivb and ivc: Discovery of a d-serine residue in co-agatoxin ivb
    • Heck, S. D., Kelbaugh, P. R., Kelly, M. E., Thadeio, P. F., Saccomano, N. A., Stroh, J. G., and Volkmann, R. A., Disulfide bond assignment of co-agatoxins IVB and IVC: Discovery of a D-serine residue in co-agatoxin IVB. J. Am. Chem. Soc., 116, 10426-10436 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10426-10436
    • Heck, S.D.1    Kelbaugh, P.R.2    Kelly, M.E.3    Thadeio, P.F.4    Saccomano, N.A.5    Stroh, J.G.6    Volkmann, R.A.7
  • 8
    • 0029935156 scopus 로고    scopus 로고
    • Posttranslational amino acid epimerization: Enzyme-catalyzed isomerization of amino acid residues in peptide chains
    • Heck, S. D., Faraci, W. S., Kelbaugh, P. R., Saccomano, N. A., Thadeio, P. F., and Volkmann, R. A., Posttranslational amino acid epimerization: Enzyme-catalyzed isomerization of amino acid residues in peptide chains. Proc. Natl. Acad. Sci. USA, 93, 4036-4039 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4036-4039
    • Heck, S.D.1    Faraci, W.S.2    Kelbaugh, P.R.3    Saccomano, N.A.4    Thadeio, P.F.5    Volkmann, R.A.6
  • 10
    • 0028236119 scopus 로고
    • Structures of the //-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, izd-mb-0503, bm-n)
    • Kubelka, V., Altmann, F., Kornfeld, G., and Marz, L., Structures of the //-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N). Arch. Biochem. Biophys., 308, 148-157 (1994).
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 148-157
    • Kubelka, V.1    Altmann, F.2    Kornfeld, G.3    Marz, L.4
  • 11
    • 0029971864 scopus 로고    scopus 로고
    • Core sugar residues of the n-linked oligosaccharides of russell’s viper venom factor x-aetivator maintain functionally active polypeptide structure
    • Gowda, D. C., Jackson, C. M., Kurzban, G. P., McPhie, P., and Davidson, E. A., Core sugar residues of the N-linked oligosaccharides of Russell’s viper venom factor X-aetivator maintain functionally active polypeptide structure. Biochemistry, 35, 5833-5837 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5833-5837
    • Gowda, D.C.1    Jackson, C.M.2    Kurzban, G.P.3    Mc Phie, P.4    Davidson, E.A.5
  • 13
    • 0025236814 scopus 로고
    • Separation of oligoman-nose-type sugar chains having one to five mannose residues by high-performance liquid chromatography as thier pyridylamino derivatives
    • Oku, H., Hase, S., and Ikenaka, T., Separation of oligoman-nose-type sugar chains having one to five mannose residues by high-performance liquid chromatography as thier pyridylamino derivatives. Anal. Biochem., 185, 331-334 (1990).
    • (1990) Anal. Biochem , vol.185 , pp. 331-334
    • Oku, H.1    Hase, S.2    Ikenaka, T.3
  • 14
    • 0023656627 scopus 로고
    • Fluorescence method for the structural analysis of oligomannose-type sugar chains by partial acetolysis
    • Natsuka, S., Hase, S., and Ikenaka, T., Fluorescence method for the structural analysis of oligomannose-type sugar chains by partial acetolysis. Anal. Biochem., 167, 154-159 (1987).
    • (1987) Anal. Biochem , vol.167 , pp. 154-159
    • Natsuka, S.1    Hase, S.2    Ikenaka, T.3
  • 15
    • 0026734854 scopus 로고
    • Distinct iv-glycan fucosylation potentials of three lepidopteran cell lines
    • Staudacher, E., Kubelka, V., and Marz, L., Distinct iV-glycan fucosylation potentials of three lepidopteran cell lines. Eur. J. Biochem., 207, 987-993 (1992).
    • (1992) Eur. J. Biochem , vol.207 , pp. 987-993
    • Staudacher, E.1    Kubelka, V.2    Marz, L.3
  • 16
    • 0025477749 scopus 로고
    • Improved method for fluorescence labeling of sugar chains with sialic acid residues
    • Kondo, A., Suzuki, J., Kuraya, N., Hase, S., Kato, I., and Ikenaka, T., Improved method for fluorescence labeling of sugar chains with sialic acid residues. Agric. Biol. Chem., 54, 2169-2170 (1990).
    • (1990) Agric. Biol. Chem , vol.54 , pp. 2169-2170
    • Kondo, A.1    Suzuki, J.2    Kuraya, N.3    Hase, S.4    Kato, I.5    Ikenaka, T.6
  • 17
    • 0029927882 scopus 로고    scopus 로고
    • Large scale preparation of pa-oligosaccharides from glycoproteins using an improved extraction method
    • Tokugawa, K., Oguri, S., and Takeuchi, M., Large scale preparation of PA-oligosaccharides from glycoproteins using an improved extraction method. Glycoconjugate /., 13, 53-56 (1996).
    • (1996) Glycoconjugate , vol.13 , pp. 53-56
    • Tokugawa, K.1    Oguri, S.2    Takeuchi, M.3
  • 18
    • 0028325772 scopus 로고
    • High-ph anion-exchange chromatography of glycoprotein-derived carbohydrates
    • Hardy, M. R., Townsend, R. R., High-pH anion-exchange chromatography of glycoprotein-derived carbohydrates. Methods En-zymol., 230,208-225 (1994).
    • (1994) Methods En-Zymol. , vol.230 , pp. 208-225
    • Hardy, M.R.1    Townsend, R.R.2
  • 19
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T., and Ikenaka, T., Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem., 95, 197-203 (1984).
    • (1984) J. Biochem , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 20
    • 0028880654 scopus 로고
    • Purification of 2-aminopyridine derivatives of oligosaccharides and related compounds by cation-exchange chromatography
    • Fan, J.-Q., Huynh, L. H., and Lee, Y. C., Purification of 2-aminopyridine derivatives of oligosaccharides and related compounds by cation-exchange chromatography. Anal. Biochem., 232, 65-68 (1995).
    • (1995) Anal. Biochem , vol.232 , pp. 65-68
    • Fan, J.-Q.1    Huynh, L.H.2    Lee, Y.C.3
  • 21
    • 0022744765 scopus 로고
    • Structure of a sugar chain of a protease inhibitor isolated from barbados pride (Caesalpinia pulcherrima sw.) seeds
    • Hase, S., Koyama, S., Daiyasu, H., Takemoto, H., Hara, S., Kobayashi, Y., Kyogoku, Y., and Ikenaka, T., Structure of a sugar chain of a protease inhibitor isolated from Barbados Pride (Caesalpinia pulcherrima Sw.) seeds. J. Biochem., 100, 1-10 (1986).
    • (1986) J. , vol.100 , pp. 1-10
    • Hase, S.1    Koyama, S.2    Daiyasu, H.3    Takemoto, H.4    Hara, S.5    Kobayashi, Y.6    Kyogoku, Y.7    Ikenaka, T.8
  • 22
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. Iv-acetylglucosaminyltransferase i and ii activities in cultured lepidopteran cells
    • Altmann, F., Kornfeld, G., Dalik, T., Staudacher, E., and Glossl, J., Processing of asparagine-linked oligosaccharides in insect cells. iV-Acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology, 3, 619-625 (1993).
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glossl, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.