메뉴 건너뛰기




Volumn 126, Issue 4, 2000, Pages 561-569

Enzymatic properties of sialidase from the ovary of the starfish, Asterina pectinifera

Author keywords

Asterina pectinifera; Effect of inhibitors; Enzymatic property; Neuraminidase; Ovary of starfish; Sialidase

Indexed keywords

SIALIDASE;

EID: 0033856893     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(00)00226-1     Document Type: Article
Times cited : (3)

References (22)
  • 1
    • 0015380932 scopus 로고
    • An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant Blue
    • Dizel, W., Kopperschlager, G., Hofmann, E., 1972. An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant Blue. Anal. Biochem. 48, 617-620.
    • (1972) Anal. Biochem. , vol.48 , pp. 617-620
    • Dizel, W.1    Kopperschlager, G.2    Hofmann, E.3
  • 2
    • 0022786352 scopus 로고
    • Purification and properties of GM1 ganglioside β-galactosidases from bovine brain
    • Hiraiwa, M., Uda, Y., 1986. Purification and properties of GM1 ganglioside β-galactosidases from bovine brain. J. Biochem. 100, 707-715.
    • (1986) J. Biochem. , vol.100 , pp. 707-715
    • Hiraiwa, M.1    Uda, Y.2
  • 3
    • 0023187275 scopus 로고
    • Human placental sialidase: Partial purification and characterization
    • Hiraiwa, M., Uda, Y., Nishizawa, M., Miyatake, T., 1987. Human placental sialidase: Partial purification and characterization. J. Biochem. 101, 1273-1279.
    • (1987) J. Biochem. , vol.101 , pp. 1273-1279
    • Hiraiwa, M.1    Uda, Y.2    Nishizawa, M.3    Miyatake, T.4
  • 4
    • 0023879371 scopus 로고
    • Human placental sialidase: Further purification and characterization
    • Hiraiwa, M., Nishizawa, M., Uda, Y., Nakajima, T., Miyatake, T., 1988. Human placental sialidase: Further purification and characterization. J. Biochem. 103, 86-90.
    • (1988) J. Biochem. , vol.103 , pp. 86-90
    • Hiraiwa, M.1    Nishizawa, M.2    Uda, Y.3    Nakajima, T.4    Miyatake, T.5
  • 5
    • 0031975165 scopus 로고    scopus 로고
    • Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts
    • Igdoura, S.A., Gafuik, C., Mertineit, C., et al., 1998. Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts. Human Mol. Genet. 7, 115-121.
    • (1998) Human Mol. Genet. , vol.7 , pp. 115-121
    • Igdoura, S.A.1    Gafuik, C.2    Mertineit, C.3
  • 6
    • 0343487873 scopus 로고    scopus 로고
    • Effects of cell surface ganglioside sialidase inhibition on growth control and differen-tiation of human neuroblastoma cells
    • Kopitz, J., Muhl, C., Ehemann, V., Lehmann, C., Cantz, M., 1997. Effects of cell surface ganglioside sialidase inhibition on growth control and differen-tiation of human neuroblastoma cells. Eur. J. Cell Biol. 73, 1-9.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 1-9
    • Kopitz, J.1    Muhl, C.2    Ehemann, V.3    Lehmann, C.4    Cantz, M.5
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 0019492995 scopus 로고
    • Ultrasensitive stain for protein in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins
    • Meril, C.R., Goldman, D., Sedman, S.A., Ebert, M.H., 1981. Ultrasensitive stain for protein in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science 211, 1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Meril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 9
    • 0021279238 scopus 로고
    • Rat liver lysosomal sialidase: Solubilization, substrate specificity and comparison with the cytosolic sialidase
    • Miyagi, T., Tsuiki, S., 1984. Rat liver lysosomal sialidase: Solubilization, substrate specificity and comparison with the cytosolic sialidase. Eur. J. Biochem. 141, 75-81.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 75-81
    • Miyagi, T.1    Tsuiki, S.2
  • 10
    • 0021808696 scopus 로고
    • Purification and characterization of cytosolic sialidase from rat liver
    • Miyagi, T., Tsuiki, S., 1985. Purification and characterization of cytosolic sialidase from rat liver. J. Biol. Chem. 260, 6710-6716.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6710-6716
    • Miyagi, T.1    Tsuiki, S.2
  • 11
    • 0025293646 scopus 로고
    • Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain
    • Miyagi, T., Segawa, J., Konno, K., Hannda, S., Tsuiki, S., 1990. Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain. J. Biochem. 107, 787-793.
    • (1990) J. Biochem. , vol.107 , pp. 787-793
    • Miyagi, T.1    Segawa, J.2    Konno, K.3    Hannda, S.4    Tsuiki, S.5
  • 12
    • 0025153582 scopus 로고
    • Generation of affinity for antithrombin III by supplemental sulfation of heparin species with low affinity for the protein
    • Tokyo
    • Ogamo, A., Metori, A., Uchiyama, H., Nagasawa, K., 1990. Generation of affinity for antithrombin III by supplemental sulfation of heparin species with low affinity for the protein. J. Biochem. (Tokyo) 108, 588-592.
    • (1990) J. Biochem. , vol.108 , pp. 588-592
    • Ogamo, A.1    Metori, A.2    Uchiyama, H.3    Nagasawa, K.4
  • 13
    • 0003879480 scopus 로고
    • Biological roles of sialic acid
    • Rosenberg, A., Schengrund, C.L. (Eds.), Plenum Press, New York
    • Rosenberg, A., Schengrund, C.L., 1976. Biological roles of sialic acid. In: Rosenberg, A., Schengrund, C.L. (Eds.), Sialidases. Plenum Press, New York.
    • (1976) Sialidases
    • Rosenberg, A.1    Schengrund, C.L.2
  • 14
    • 0003631621 scopus 로고
    • Biology of the sialic acids
    • Rosenberg, A. (Ed.), Plenum Press, New York
    • Saito, M., Yu, R.K., 1995. Biology of the sialic acids. In: Rosenberg, A. (Ed.), Biochemistry and Function of Sialic Acid. Plenum Press, New York.
    • (1995) Biochemistry and Function of Sialic Acid
    • Saito, M.1    Yu, R.K.2
  • 15
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological function of sialic acids
    • Academic Press, New York
    • Schauer, R., 1982. Chemistry, metabolism, and biological function of sialic acids. In: Advances in Carbohydrate Chemistry and Biochemistry, vol. 40. Academic Press, New York.
    • (1982) Advances in Carbohydrate Chemistry and Biochemistry , vol.40
    • Schauer, R.1
  • 16
    • 0024635544 scopus 로고
    • Isolation and characterization of sialidase from the starfish Asterina rubens
    • Schauer, R., Wember, M., 1989. Isolation and characterization of sialidase from the starfish Asterina rubens. Biol. Chem. Hoppe-Seyler 370, 183-190.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 183-190
    • Schauer, R.1    Wember, M.2
  • 17
    • 0026180780 scopus 로고
    • Lysosomal and plasma membrane ganglioside GM3 sialidase of cultured human fibroblasts: Differentiation by detergents and inhibitors
    • Schneider-Jakob, H.R., Cantz, M., 1991. Lysosomal and plasma membrane ganglioside GM3 sialidase of cultured human fibroblasts: Differentiation by detergents and inhibitors. Biol. Chem. Hoppe-Seyler 372, 443-450.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 443-450
    • Schneider-Jakob, H.R.1    Cantz, M.2
  • 18
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith, P.K., Krohn, R.I., Hermanson, G.T., et al., 1985. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
    • (1985) Anal. Biochem. , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 19
    • 0345607040 scopus 로고    scopus 로고
    • Purification and characterization of sialidase from starfish, Asterina pectinifera
    • Sapporo Med. Univ.
    • Takeuchi, N., Saitoh, M., Shiraishi, T., et al., 1996. Purification and characterization of sialidase from starfish, Asterina pectinifera. Bull. Marine Biomed. Inst, Sapporo Med. Univ. 3, 55-61.
    • (1996) Bull. Marine Biomed. Inst , vol.3 , pp. 55-61
    • Takeuchi, N.1    Saitoh, M.2    Shiraishi, T.3
  • 20
    • 0024330314 scopus 로고
    • Molecular cloning of a full-length cDNA for human α-N-acetylgalactosaminidase (α-galactosidase B)
    • Tsuji, S., Yamauchi, T., Hiraiwa, M., et al., 1989. Molecular cloning of a full-length cDNA for human α-N-acetylgalactosaminidase (α-galactosidase B). Biochem. Biophys. Res. Commun. 163, 1498-1504.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 1498-1504
    • Tsuji, S.1    Yamauchi, T.2    Hiraiwa, M.3
  • 21
    • 0024495357 scopus 로고
    • Identification and in vitro reconstitution of lysosomal neuraminidase from human placenta
    • van der Horst, G.T.J., Galjart, N.J., d'Azzo, A., Galjaard, H., Verheijen, F.W., 1989. Identification and in vitro reconstitution of lysosomal neuraminidase from human placenta. J. Biol. Chem. 264, 1317-1322.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1317-1322
    • Van Der Horst, G.T.J.1    Galjart, N.J.2    D'Azzo, A.3    Galjaard, H.4    Verheijen, F.W.5
  • 22
    • 0029871790 scopus 로고    scopus 로고
    • Two different sialidases, KDN-sialidase and regular sialidase, in the starfish Asterina pectinifera
    • Yuziuk, J.A., Nakagawa, H., Hasegawa, A., Kiso, M., Li, S.-C., Li, Y.-T., 1996. Two different sialidases, KDN-sialidase and regular sialidase, in the starfish Asterina pectinifera. Biochem. J. 315, 1041-1048.
    • (1996) Biochem. J. , vol.315 , pp. 1041-1048
    • Yuziuk, J.A.1    Nakagawa, H.2    Hasegawa, A.3    Kiso, M.4    Li, S.-C.5    Li, Y.-T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.