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Volumn 79, Issue 2, 1996, Pages 198-204

Purification of the Bovine Xanthine Oxidoreductase from Milk Fat Globule Membranes and Cloning of Complementary Deoxyribonucleic Acid

Author keywords

Bovine; Complementary deoxyribonucleic acid; Protein; Xanthine oxidoreductase

Indexed keywords

BOVINAE; MAMMALIA;

EID: 0030077060     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(96)76351-8     Document Type: Article
Times cited : (61)

References (27)
  • 2
    • 0026553672 scopus 로고
    • PROSITE: A dictionary of sites of patterns in proteins
    • Bairoch, A. 1992. PROSITE: a dictionary of sites of patterns in proteins. Nucleic Acid Res. 20:2013.
    • (1992) Nucleic Acid Res. , vol.20 , pp. 2013
    • Bairoch, A.1
  • 3
    • 0017367397 scopus 로고
    • Screening lambda gt recombinant clones by hybridization to single plaques in situ
    • Benton, W. D., and R. W. Davis. 1977. Screening lambda gt recombinant clones by hybridization to single plaques in situ. Science 196:180.
    • (1977) Science , vol.196 , pp. 180
    • Benton, W.D.1    Davis, R.W.2
  • 4
    • 0019631539 scopus 로고
    • Sulfhydryl oxidase-catalyzed conversion of xanthine dehydrogenase to xanthine oxidase
    • Clare, D. A., B. A. Blakistone, H. E. Swaisgood, and H. R. Horton. 1981. Sulfhydryl oxidase-catalyzed conversion of xanthine dehydrogenase to xanthine oxidase. Arch. Biochem. Biophys. 211:44.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 44
    • Clare, D.A.1    Blakistone, B.A.2    Swaisgood, H.E.3    Horton, H.R.4
  • 5
    • 0014294662 scopus 로고
    • The regulation of xanthine oxidase in rat liver: Modification of the enzyme activity of rat liver supernatant on storage at 20°C
    • Della Corte, E., and F. Stirpe. 1968. The regulation of xanthine oxidase in rat liver: modification of the enzyme activity of rat liver supernatant on storage at 20°C. Biochem. J. 108:349.
    • (1968) Biochem. J. , vol.108 , pp. 349
    • Della Corte, E.1    Stirpe, F.2
  • 6
    • 0027438935 scopus 로고
    • Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): Structural analysis of the protein and chromosomal location of the gene
    • Ichida, K., Y. Amaya, K. Noda, S. Minoshima, T. Hosoya, O. Sakai, N. Shimizu, and T. Nishino. 1993. Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene 133:279.
    • (1993) Gene , vol.133 , pp. 279
    • Ichida, K.1    Amaya, Y.2    Noda, K.3    Minoshima, S.4    Hosoya, T.5    Sakai, O.6    Shimizu, N.7    Nishino, T.8
  • 7
    • 0026695884 scopus 로고
    • Subcellular localization of xanthine oxidase in rat hepatocytes: High-resolution immunoelectron microscopic study combined with biochemical analysis
    • Ichikawa, M., T. Nishino, T. Nishino, and A. Ichikawa. 1992. Subcellular localization of xanthine oxidase in rat hepatocytes: high-resolution immunoelectron microscopic study combined with biochemical analysis. J. Histochem. Cytochem. 40.1097.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1097
    • Ichikawa, M.1    Nishino, T.2    Nishino, T.3    Ichikawa, A.4
  • 8
    • 0019414648 scopus 로고
    • Localization of xanthine oxidase in mammary gland epithelium and capillary endothelium
    • Jarasch, E.-D., C. Grund, G. Bruder, H. W. Heid, T. W. Keenan, and W. W. Franke. 1981. Localization of xanthine oxidase in mammary gland epithelium and capillary endothelium. Cell 25:67.
    • (1981) Cell , vol.25 , pp. 67
    • Jarasch, E.-D.1    Grund, C.2    Bruder, G.3    Heid, H.W.4    Keenan, T.W.5    Franke, W.W.6
  • 9
    • 0040743999 scopus 로고
    • Secretory membranes of the lactating mammary gland
    • Kanno, C. 1990. Secretory membranes of the lactating mammary gland. Protoplasma 159:184.
    • (1990) Protoplasma , vol.159 , pp. 184
    • Kanno, C.1
  • 10
    • 0023333651 scopus 로고
    • Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster
    • Keith, T. P., M. A. Riley, M. Kreitman, R. C. Lewontin, D. Curtis, and G. Chambers. 1987. Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster. Genetics 116:67.
    • (1987) Genetics , vol.116 , pp. 67
    • Keith, T.P.1    Riley, M.A.2    Kreitman, M.3    Lewontin, R.C.4    Curtis, D.5    Chambers, G.6
  • 11
    • 84976110984 scopus 로고
    • Milk enzymes - Their distribution and activity
    • Kitchen, B. J., G. C. Taylor, and I. C. White. 1970. Milk enzymes - their distribution and activity. J. Dairy Res. 37:279.
    • (1970) J. Dairy Res. , vol.37 , pp. 279
    • Kitchen, B.J.1    Taylor, G.C.2    White, I.C.3
  • 12
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: Intimations of translational control
    • Kozak, M. 1991. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115:887.
    • (1991) J. Cell Biol. , vol.115 , pp. 887
    • Kozak, M.1
  • 14
    • 0019195899 scopus 로고
    • Separation of the proteins of bovine milk-fat-globule-membrane by electrophoresis with retention of the enzymatic and immunological activity
    • Mather, I. H., C. B. Tramplin, and M. G. Irving. 1980. Separation of the proteins of bovine milk-fat-globule-membrane by electrophoresis with retention of the enzymatic and immunological activity. Eur. J. Biochem. 110:327.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 327
    • Mather, I.H.1    Tramplin, C.B.2    Irving, M.G.3
  • 15
    • 0017261771 scopus 로고
    • Subunit structure of bovine milk xanthine oxidase
    • Nagler, L. G., and L. S. Vartanyan. 1976. Subunit structure of bovine milk xanthine oxidase. Biochim. Biophys. Acta 427:78.
    • (1976) Biochim. Biophys. Acta , vol.427 , pp. 78
    • Nagler, L.G.1    Vartanyan, L.S.2
  • 16
    • 0028069815 scopus 로고
    • The conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury
    • Nishino, T. 1994. The conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury. J. Biochem. (Tokyo) 116:1.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 1
    • Nishino, T.1
  • 17
    • 0024556882 scopus 로고
    • The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase
    • Nishino, T., and T. Nishino. 1989. The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. J. Biol. Chem. 264:5468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5468
    • Nishino, T.1    Nishino, T.2
  • 18
    • 0019892010 scopus 로고
    • Purification of highly active milk xanthine oxidase by affinity chromatography on sepharose 4B/folate gel
    • Nishino, T., T. Nishino, and K. Tsushima. 1981. Purification of highly active milk xanthine oxidase by affinity chromatography on sepharose 4B/folate gel. FEBS (Fed. Eur. Biol. Soc.) Lett. 131:369.
    • (1981) FEBS (Fed. Eur. Biol. Soc.) Lett. , vol.131 , pp. 369
    • Nishino, T.1    Nishino, T.2    Tsushima, K.3
  • 19
    • 0022502428 scopus 로고
    • Xanthine oxidase: Biochemistry, distribution and physiology
    • Parks, D. A., and D. N. Granger. 1986. Xanthine oxidase: biochemistry, distribution and physiology. Acta Physiol. Scand. Suppl. 548:87.
    • (1986) Acta Physiol. Scand. Suppl. , vol.548 , pp. 87
    • Parks, D.A.1    Granger, D.N.2
  • 20
  • 22
    • 0019210886 scopus 로고
    • Xanthine oxidase: An enzyme playing a role in the killing mechanism of polymorphonuclear leucocytes
    • Tubaro, E., B. Lotti, C. Santiangeli, and G. Cavallo. 1980. Xanthine oxidase: an enzyme playing a role in the killing mechanism of polymorphonuclear leucocytes. Biochem. Pharmacol. 29:3018.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 3018
    • Tubaro, E.1    Lotti, B.2    Santiangeli, C.3    Cavallo, G.4
  • 24
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding beta-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpstra, and W. G. Hol. 1986. Prediction of the occurrence of the ADP-binding beta-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 25
    • 0017734449 scopus 로고
    • Distribution of xanthine oxidase and xanthine dehydrogenase among bacteria
    • Woolfolk, C., and J. S. Downard. 1977. Distribution of xanthine oxidase and xanthine dehydrogenase among bacteria. J. Bacteriol. 130:1175.
    • (1977) J. Bacteriol. , vol.130 , pp. 1175
    • Woolfolk, C.1    Downard, J.S.2
  • 26
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • Wootton, J. C., R. E. Nicolson, J. M. Cock, D. E. Walters, J. F. Burke, W. A. Doyle, and R. C. Bray. 1991. Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim. Biophys. Acta 1057:157.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.