메뉴 건너뛰기




Volumn 380, Issue 1, 2004, Pages 211-218

Partial amino acid sequence and mRNA analysis of cytosolic pyridoxine-β-D-glucoside hydrolase from porcine intestinal mucosa: Proposed derivation from the lactase-phlorizin hydrolase gene

Author keywords

Absorption; Bioavailability; Intestinal mucosa; Lactase phlorizin hydrolase (LPH); Pyridoxine D glucoside hydrolase (PNGH); Vitamin B6

Indexed keywords

AMINO ACIDS; DERIVATIVES; ENZYMES; GENES; HYDROLYSIS;

EID: 2642527770     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031416     Document Type: Article
Times cited : (4)

References (34)
  • 1
    • 0001464420 scopus 로고
    • The determination of pyridoxine-β-glucoside bioavailability in the rat
    • Ink, S. L., Gregory, J. F. and Sartain, D. B. (1986) The determination of pyridoxine-β-glucoside bioavailability in the rat. J. Agric. Food Chem. 34, 857-862
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 857-862
    • Ink, S.L.1    Gregory, J.F.2    Sartain, D.B.3
  • 3
    • 0025731533 scopus 로고
    • Bioavailability of pyridoxine-5′-β-D-glucoside determined in humans by stable-isotopic methods
    • Gregory, J. F., Trumbo, P. R., Bailey, L. B., Toth, J. P., Baumgartner, T. G. and Cerda, J. J. (1991) Bioavailability of pyridoxine-5′-β-D- glucoside determined in humans by stable-isotopic methods. J. Nutr. 121, 177-186
    • (1991) J. Nutr. , vol.121 , pp. 177-186
    • Gregory, J.F.1    Trumbo, P.R.2    Bailey, L.B.3    Toth, J.P.4    Baumgartner, T.G.5    Cerda, J.J.6
  • 4
    • 0030763914 scopus 로고    scopus 로고
    • 6 and partially inhibits the utilization of co-ingested pyridoxine in humans
    • 6 and partially inhibits the utilization of co-ingested pyridoxine in humans. J. Nutr. 127, 1508-1513
    • (1997) J. Nutr. , vol.127 , pp. 1508-1513
    • Nakano, H.1    McMahon, L.G.2    Gregory, J.F.3
  • 6
    • 0005787427 scopus 로고
    • Molecular biology and enzymology of human acid β-glucosidase
    • Esen, A., ed., American Chemical Society, Washington D.C.
    • Grabowski, G. A., Berg-Fussman, A. and Grace, M. (1993) Molecular biology and enzymology of human acid β-glucosidase. In β-Glucosidase: Biochemistry and Molecular Biology (Esen, A., ed.), pp. 66-82, American Chemical Society, Washington D.C.
    • (1993) β-Glucosidase: Biochemistry and Molecular Biology , pp. 66-82
    • Grabowski, G.A.1    Berg-Fussman, A.2    Grace, M.3
  • 7
    • 0035070246 scopus 로고    scopus 로고
    • Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase
    • Naim, H. Y. (2001) Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase. Histol. Histopathol. 16, 553-561
    • (2001) Histol. Histopathol. , vol.16 , pp. 553-561
    • Naim, H.Y.1
  • 8
    • 0002206919 scopus 로고
    • The mammalian cytosolic broad-specificity β-glucosidase
    • Esen, A., ed., American Chemical Society, Washington D.C.
    • Glew, R. H., Gopalan, V., Forsyth, G. W. and VanderJagt, D. J. (1993) The mammalian cytosolic broad-specificity β-glucosidase. In β-Glucosidase: Biochemistry and Molecular Biology (Esen, A., ed.), pp. 83-112, American Chemical Society, Washington D.C.
    • (1993) β-Glucosidase: Biochemistry and Molecular Biology , pp. 83-112
    • Glew, R.H.1    Gopalan, V.2    Forsyth, G.W.3    VanderJagt, D.J.4
  • 9
    • 0025135095 scopus 로고
    • Hydrolysis of pyridoxine-5′-β-D-glucoside by a broad-specificity β-glucosidase from mammalian tissues
    • Trumbo, P. R., Banks, M. A. and Gregory, J. F. (1990) Hydrolysis of pyridoxine-5′-β-D-glucoside by a broad-specificity β-glucosidase from mammalian tissues. Proc. Soc. Exp. Biol. Med. 195, 240-246
    • (1990) Proc. Soc. Exp. Biol. Med. , vol.195 , pp. 240-246
    • Trumbo, P.R.1    Banks, M.A.2    Gregory, J.F.3
  • 10
    • 2642580303 scopus 로고
    • Isolation and properties of pyridoxine-5′-β-D-glucosidase from pig intestine mucosa
    • Nakano, H., Levy, M. D. and Gregory, J. F. (1995) Isolation and properties of pyridoxine-5′-β-D-glucosidase from pig intestine mucosa. FASEB J. 9, A986
    • (1995) FASEB J. , vol.9
    • Nakano, H.1    Levy, M.D.2    Gregory, J.F.3
  • 11
    • 0031436636 scopus 로고    scopus 로고
    • Cytosolic pyridoxine-β-D-glucoside hydrolase from porcine jejunal mucosa. Purification, properties, and comparison with broad specificity β-glucosidase
    • McMahon, L. G., Nakano, H., Levy, M. D. and Gregory, J. F. (1997) Cytosolic pyridoxine-β-D-glucoside hydrolase from porcine jejunal mucosa. Purification, properties, and comparison with broad specificity β-glucosidase. J. Biol. Chem. 272, 32025-32033
    • (1997) J. Biol. Chem. , vol.272 , pp. 32025-32033
    • McMahon, L.G.1    Nakano, H.2    Levy, M.D.3    Gregory, J.F.4
  • 12
    • 0037178825 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of pytidoxine-5′-β-D-glucoside is catalyzed by intestinal lactase-phlorizin hydrolase
    • Mackey, A. D., Henderson, G. N. and Gregory, J. F. (2002) Enzymatic hydrolysis of pytidoxine-5′-β-D-glucoside is catalyzed by intestinal lactase-phlorizin hydrolase. J. Biol. Chem. 277, 26858-26864
    • (2002) J. Biol. Chem. , vol.277 , pp. 26858-26864
    • Mackey, A.D.1    Henderson, G.N.2    Gregory, J.F.3
  • 13
    • 0019857253 scopus 로고
    • The glycosylceramidase in the murine intestine: Purification and substrate specificity
    • Kobayashi, T. and Suzuki, K. (1981) The glycosylceramidase in the murine intestine: purification and substrate specificity. J. Biol. Chem, 256, 7768-7773
    • (1981) J. Biol. Chem , vol.256 , pp. 7768-7773
    • Kobayashi, T.1    Suzuki, K.2
  • 15
    • 0025823166 scopus 로고
    • Expression of a full-length cDNA coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein
    • Naim, H. Y., Lacey, S. W., Sambrook, J. F. and Gething, M.-J. H. (1991) Expression of a full-length cDNA coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein. J. Biol. Chem. 266, 12313-12320
    • (1991) J. Biol. Chem. , vol.266 , pp. 12313-12320
    • Naim, H.Y.1    Lacey, S.W.2    Sambrook, J.F.3    Gething, M.-J.H.4
  • 16
    • 0029281959 scopus 로고
    • The pro-region of human intestinal lactase-phorizin hydrolase is enzymatically inactive towards lactose
    • Naim, H. Y. (1995) The pro-region of human intestinal lactase-phorizin hydrolase is enzymatically inactive towards lactose. Biol. Chem. 376, 255-258
    • (1995) Biol. Chem. , vol.376 , pp. 255-258
    • Naim, H.Y.1
  • 17
    • 0028148546 scopus 로고
    • The pro region of human intestinal lactase-phlorizin hydrolase
    • Naim, H. Y., Jacob, R., Naim, H., Sambrook, J. F. and Gething, M.-J. H. (1994) The pro region of human intestinal lactase-phlorizin hydrolase. J. Biol. Chem. 269, 26933-26943
    • (1994) J. Biol. Chem. , vol.269 , pp. 26933-26943
    • Naim, H.Y.1    Jacob, R.2    Naim, H.3    Sambrook, J.F.4    Gething, M.-J.H.5
  • 18
    • 0025882118 scopus 로고
    • Structure of the chromosomal gene and cDNAs coding for lactase-phlorizin hydrolase in humans with adult-type hypolactasia or persistence of lactase
    • Boll, O. W., Wagner, P. and Mantei, N. (1991) Structure of the chromosomal gene and cDNAs coding for lactase-phlorizin hydrolase in humans with adult-type hypolactasia or persistence of lactase. Am. J. Hum. Genet. 48, 889-902
    • (1991) Am. J. Hum. Genet. , vol.48 , pp. 889-902
    • Boll, O.W.1    Wagner, P.2    Mantei, N.3
  • 19
    • 0024076253 scopus 로고
    • Complete primary structure of human and rabbit lactase-phlorizin hydrolase: Implications for biosynthesis, membrane anchoring and evolution of the enzyme
    • Mantei, N., Villa, M., Enzler, T., Wacker, H., Boll, W., Hunziker, W. and Semenza, G. (1988) Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme. EMBO J. 7, 2705-2713
    • (1988) EMBO J. , vol.7 , pp. 2705-2713
    • Mantei, N.1    Villa, M.2    Enzler, T.3    Wacker, H.4    Boll, W.5    Hunziker, W.6    Semenza, G.7
  • 20
    • 0031411221 scopus 로고    scopus 로고
    • Preparation of nonlabeled, tritiated, and deuterated pyridoxine 5′-β-D-glucoside and assay of pyridoxine-5′-β-D-glucoside hydrolase
    • Gregory, J. F. and Nakano, H. (1997) Preparation of nonlabeled, tritiated, and deuterated pyridoxine 5′-β-D-glucoside and assay of pyridoxine-5′-β-D-glucoside hydrolase. Methods Enzymol. 280, 58-65
    • (1997) Methods Enzymol. , vol.280 , pp. 58-65
    • Gregory, J.F.1    Nakano, H.2
  • 21
    • 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 (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0028845427 scopus 로고
    • Pyridoxine and pyridoxine-5′-β-D-glucoside exert different effects on tissue B-6 vitamers but similar effects on β-glucosidase activity in rats
    • Nakano, H. and Gregory, J. F. (1995) Pyridoxine and pyridoxine-5′- β-D-glucoside exert different effects on tissue B-6 vitamers but similar effects on β-glucosidase activity in rats. J. Nutr. 125, 2751-2762
    • (1995) J. Nutr. , vol.125 , pp. 2751-2762
    • Nakano, H.1    Gregory, J.F.2
  • 23
    • 0019751507 scopus 로고
    • Protein determination in membrane and lipoprotein samples: Manual and automated procedures
    • Markwell, M. A., Haas, S. M., Tolbert, N. E. and Bieber, L. L. (1981) Protein determination in membrane and lipoprotein samples: manual and automated procedures. Methods Enzymol. 72, 296-303
    • (1981) Methods Enzymol. , vol.72 , pp. 296-303
    • Markwell, M.A.1    Haas, S.M.2    Tolbert, N.E.3    Bieber, L.L.4
  • 24
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld, J., Capdevielle, J., Guillemot, J. C. and Ferrara, P. (1992) In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203, 173-179
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 25
    • 0036629207 scopus 로고    scopus 로고
    • Synthesis and characterization of a collagen model δ-O- phosphohydroxylysine-containing peptide
    • Hubalek, F., Edmondson, D. E. and Pohl, J. (2002) Synthesis and characterization of a collagen model δ-O-phosphohydroxylysine-containing peptide. Anal. Biochem. 306, 124-134
    • (2002) Anal. Biochem. , vol.306 , pp. 124-134
    • Hubalek, F.1    Edmondson, D.E.2    Pohl, J.3
  • 26
  • 27
    • 0030188330 scopus 로고    scopus 로고
    • Evaluation and characterization of a porcine small intestine cDNA library: Analysis of 839 clones
    • Winterø, A. K., Fredholm, M. and Davies, W. (1996) Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones. Mamm. Genome 7, 509-517
    • (1996) Mamm. Genome , vol.7 , pp. 509-517
    • Winterø, A.K.1    Fredholm, M.2    Davies, W.3
  • 29
    • 0026516892 scopus 로고
    • One-hour downward alkaline capillary transfer for blotting of DNA and RNA
    • Chomczynsky, P. (1992) One-hour downward alkaline capillary transfer for blotting of DNA and RNA. Anal. Biochem. 201, 134-139
    • (1992) Anal. Biochem. , vol.201 , pp. 134-139
    • Chomczynsky, P.1
  • 30
    • 0032513204 scopus 로고    scopus 로고
    • The 67-kDa enzymatically inactive alternatively spliced variant of β-galactosidase is identical to the elastin/laminin-binding protein
    • Privitera, S., Prody, C. A., Callahan, J. W. and Hinek, A. (1998) The 67-kDa enzymatically inactive alternatively spliced variant of β-galactosidase is identical to the elastin/laminin-binding protein. J. Biol. Chem, 273, 6319-6326
    • (1998) J. Biol. Chem , vol.273 , pp. 6319-6326
    • Privitera, S.1    Prody, C.A.2    Callahan, J.W.3    Hinek, A.4
  • 31
    • 0024367979 scopus 로고
    • Alternative splicing of β-galactosidase mRNA generates the classic lysosomal enzyme and a β-galactosidase-related protein
    • Morreau, H., Galjart, N. J., Gillemans, N., Willemsen, R., van der Horst, G. T. and d'Azzo, A. (1989) Alternative splicing of β-galactosidase mRNA generates the classic lysosomal enzyme and a β-galactosidase-related protein. J. Biol. Chem. 264, 20655-20663
    • (1989) J. Biol. Chem. , vol.264 , pp. 20655-20663
    • Morreau, H.1    Galjart, N.J.2    Gillemans, N.3    Willemsen, R.4    Van Der Horst, G.T.5    D'Azzo, A.6
  • 33
    • 0032544605 scopus 로고    scopus 로고
    • Intestinal lactase-phlorizin hydrolase (LPH): The two catalytic sites; the role of the pancreas in pro-LPH maturation
    • Zecca, L., Mesonero, J. E., Stutz, A., Poirée, J.-C., Giudicelli, J., Cursio, R., Cloor, S. M. and Semenza, G. (1998) Intestinal lactase-phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro-LPH maturation. FEBS Lett. 435, 225-228
    • (1998) FEBS Lett. , vol.435 , pp. 225-228
    • Zecca, L.1    Mesonero, J.E.2    Stutz, A.3    Poirée, J.-C.4    Giudicelli, J.5    Cursio, R.6    Cloor, S.M.7    Semenza, G.8
  • 34
    • 0034531969 scopus 로고    scopus 로고
    • Differential mechanism-based labeling and unequivocal activity assignment of the two active sites of intestinal lactase/phlorizin hydrolase
    • Arribas, J. C., Herrero, A. G., Martin-Lomas, M., Canada, F. J., He, S. and Withers, S. G. (2000) Differential mechanism-based labeling and unequivocal activity assignment of the two active sites of intestinal lactase/phlorizin hydrolase. Eur. J. Biochem. 267, 6996-7005
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6996-7005
    • Arribas, J.C.1    Herrero, A.G.2    Martin-Lomas, M.3    Canada, F.J.4    He, S.5    Withers, S.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.