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Volumn 71, Issue 1, 2004, Pages 7-13

Goats' milk xanthine oxidoreductase is grossly deficient in molybdenum

Author keywords

Bovine; Caprine; Goat; Human; Milk; Molybdenum; Secretion; Xanthine oxidase

Indexed keywords

MOLYBDENUM; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

EID: 1642405513     PISSN: 00220299     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0022029903006514     Document Type: Article
Times cited : (34)

References (37)
  • 2
    • 0027500351 scopus 로고
    • Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial cell surface
    • Adachi T, Fukushima T, Usami Y & Hirano K 1993 Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial cell surface. Biochemical Journal 289 523-527
    • (1993) Biochemical Journal , vol.289 , pp. 523-527
    • Adachi, T.1    Fukushima, T.2    Usami, Y.3    Hirano, K.4
  • 4
    • 0002819537 scopus 로고
    • Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the cofactors and the catalytic functions of enzyme fractions from cows' milk
    • Avis PG, Bergel F & Bray RC 1956 Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the cofactors and the catalytic functions of enzyme fractions from cows' milk. Journal of the Chemical Society 1219-1225
    • (1956) Journal of the Chemical Society , pp. 1219-1225
    • Avis, P.G.1    Bergel, F.2    Bray, R.C.3
  • 6
    • 77956942930 scopus 로고
    • Molybdenum iron-sulfur flavin hydroxylases and related enzymes
    • (Ed. PD Boyer). New York: Academic Press
    • Bray RC 1975 Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In The Enzymes, Vol. XII, 3rd Edn., pp. 299-419 (Ed. PD Boyer). New York: Academic Press
    • (1975) The Enzymes, Vol. XII, 3rd Edn. , vol.12 , pp. 299-419
    • Bray, R.C.1
  • 7
    • 0002085098 scopus 로고    scopus 로고
    • Properties of xanthine oxidase from human milk: The enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulfur centres
    • (Eds S Ghisla, PMH Kroneck, P Macheroux & H Sund). Berlin: Agency for Scientific Publications
    • Bray RC, Lowe D, Godber B, Harrison R & Eisenthal R 1999 Properties of xanthine oxidase from human milk: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulfur centres. In Flavins and Flavoproteins, Proc. 13th International Symposium, Konstanz, Germany, pp. 775-778 (Eds S Ghisla, PMH Kroneck, P Macheroux & H Sund). Berlin: Agency for Scientific Publications
    • (1999) Flavins and Flavoproteins, Proc. 13th International Symposium, Konstanz, Germany , pp. 775-778
    • Bray, R.C.1    Lowe, D.2    Godber, B.3    Harrison, R.4    Eisenthal, R.5
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0018109126 scopus 로고
    • Comparison of the molybdenum centres of native and desulpho xanthine oxidase
    • Gutteridge S, Tanner SJ, Bray RC 1978 Comparison of the molybdenum centres of native and desulpho xanthine oxidase. Biochemical Journal 175 887-897
    • (1978) Biochemical Journal , vol.175 , pp. 887-897
    • Gutteridge, S.1    Tanner, S.J.2    Bray, R.C.3
  • 17
    • 0030882009 scopus 로고    scopus 로고
    • Human xanthine oxidoreductase: In search of a function
    • Harrison R 1997 Human xanthine oxidoreductase: in search of a function. Biochemical Society Transactions 25 786-791
    • (1997) Biochemical Society Transactions , vol.25 , pp. 786-791
    • Harrison, R.1
  • 18
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase: Where are we now?
    • Harrison R 2002 Structure and function of xanthine oxidoreductase: where are we now? Free Radical Biology and Medicine 33 774-797
    • (2002) Free Radical Biology and Medicine , vol.33 , pp. 774-797
    • Harrison, R.1
  • 20
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R 1996 The mononuclear molybdenum enzymes. Chemical Reviews 96 2757-2816
    • (1996) Chemical Reviews , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 21
    • 0000146015 scopus 로고
    • The extinction coefficients of the reduced band of pyridine nucleotides
    • Horecker BL & Kornberg A 1948 The extinction coefficients of the reduced band of pyridine nucleotides. Journal of Biological Chemistry 175 385-390
    • (1948) Journal of Biological Chemistry , vol.175 , pp. 385-390
    • Horecker, B.L.1    Kornberg, A.2
  • 22
    • 0035405319 scopus 로고    scopus 로고
    • Milk lipid globules and their surrounding membrane: A brief history and perspectives for future research
    • Keenan TW 2001 Milk lipid globules and their surrounding membrane: a brief history and perspectives for future research. Journal of Mammary Gland Biology and Neoplasia 6 365-371
    • (2001) Journal of Mammary Gland Biology and Neoplasia , vol.6 , pp. 365-371
    • Keenan, T.W.1
  • 23
    • 0002946615 scopus 로고
    • The structure of milk: Implications for sampling and storage. A. The milk lipid globule membrane
    • (Ed. RG Jensen). New York: Academic Press
    • Keenan TW & Patton S 1995 The structure of milk: implications for sampling and storage. A. The milk lipid globule membrane. In Handbook of Milk Composition, pp. 5-50 (Ed. RG Jensen). New York: Academic Press
    • (1995) Handbook of Milk Composition , pp. 5-50
    • Keenan, T.W.1    Patton, S.2
  • 25
    • 0000114733 scopus 로고
    • The antibacterial effect of enzymatic xanthine oxidation
    • Lipmann F & Owen CR 1943 The antibacterial effect of enzymatic xanthine oxidation. Science 98 246-248
    • (1943) Science , vol.98 , pp. 246-248
    • Lipmann, F.1    Owen, C.R.2
  • 26
    • 0030824355 scopus 로고    scopus 로고
    • Milk xanthine dehydrogenase: The first one hundred years
    • Massey V & Harris CM 1997 Milk xanthine dehydrogenase: the first one hundred years. Biochemical Society Transactions 25 750-755
    • (1997) Biochemical Society Transactions , vol.25 , pp. 750-755
    • Massey, V.1    Harris, C.M.2
  • 27
    • 0036902177 scopus 로고    scopus 로고
    • Functional regulation of xanthine oxidoreductase expression and localization in the mouse mammary gland: Evidence of a role in lipid secretion
    • McManaman JL, Palmer CA, Wright RM & Neville MC 2002 Functional regulation of xanthine oxidoreductase expression and localization in the mouse mammary gland: evidence of a role in lipid secretion. Journal of Physiology 545 567-569
    • (2002) Journal of Physiology , vol.545 , pp. 567-569
    • McManaman, J.L.1    Palmer, C.A.2    Wright, R.M.3    Neville, M.C.4
  • 30
    • 0029862597 scopus 로고    scopus 로고
    • Cloning and expression in vitro of human xanthine dehydrogenase/oxidase
    • Saksela M & Raivio KO 1996 Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochemical Journal 315 235-239
    • (1996) Biochemical Journal , vol.315 , pp. 235-239
    • Saksela, M.1    Raivio, K.O.2
  • 31
    • 0030976206 scopus 로고    scopus 로고
    • NADH oxidase activity of human xanthine oxidoreductase. Generation of superoxide anion
    • Sanders SA, Eisenthal R & Harrison R 1997 NADH oxidase activity of human xanthine oxidoreductase. Generation of superoxide anion. European Journal of Biochemistry 245 541-548
    • (1997) European Journal of Biochemistry , vol.245 , pp. 541-548
    • Sanders, S.A.1    Eisenthal, R.2    Harrison, R.3
  • 32
    • 0028893185 scopus 로고
    • The structure of chicken liver xanthine dehydrogenase, cDNA cloning and the domain structure
    • Sato A, Nishino T, Noda K, Amaya Y & Nishino T 1995 The structure of chicken liver xanthine dehydrogenase, cDNA cloning and the domain structure. Journal of Biological Chemistry 270 2818-2826
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 2818-2826
    • Sato, A.1    Nishino, T.2    Noda, K.3    Amaya, Y.4    Nishino, T.5
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T & Gordon, J 1979 Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of USA 76 4350-4357
    • (1979) Proceedings of the National Academy of Sciences of USA , vol.76 , pp. 4350-4357
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0037115712 scopus 로고    scopus 로고
    • The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: Gene sharing in the lactating mammary gland
    • Vorbach C, Striven A & Capecchi MR 2002 The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland. Genes & Development 16 3223-3235
    • (2002) Genes & Development , vol.16 , pp. 3223-3235
    • Vorbach, C.1    Striven, A.2    Capecchi, M.R.3
  • 36
    • 0020478588 scopus 로고
    • Evidence for the inorganic nature of the cyanolysable sulfur of molybdenum hydroxylases
    • Wahl RC & Rajagopalan KV 1982 Evidence for the inorganic nature of the cyanolysable sulfur of molybdenum hydroxylases. Journal of Biological Chemistry 257 1354-1359
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 1354-1359
    • Wahl, R.C.1    Rajagopalan, K.V.2
  • 37
    • 1642287291 scopus 로고
    • Bovine, caprine and human milk xanthine oxidases: Isolation, purification and characterisation
    • (Ed. G Charalambous). Orlando: Academic Press
    • Zikakis JP, Dressel MA & Silver MR 1983 Bovine, caprine and human milk xanthine oxidases: isolation, purification and characterisation. In Instrumental Analysis of Foods, Vol. 2, pp. 243-303 (Ed. G Charalambous). Orlando: Academic Press
    • (1983) Instrumental Analysis of Foods , vol.2 , pp. 243-303
    • Zikakis, J.P.1    Dressel, M.A.2    Silver, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.