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Volumn 372, Issue 2, 2003, Pages 443-451

Biochemical and mass spectrometric characterization of soluble ecto-5′-nucleotidase from bull seminal plasma

Author keywords

Glycosylphosphatidylinositol anchor; Membrane; MS; Soluble ecto 5 nucleotidase

Indexed keywords

BIOCHEMISTRY; BIOLOGICAL MEMBRANES; DRUG PRODUCTS; OLIGOMERS; POLYPEPTIDES; TISSUE;

EID: 0038676998     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021687     Document Type: Article
Times cited : (28)

References (30)
  • 1
    • 0026729643 scopus 로고
    • 5′-nucleotidase: Molecular structure and functional aspects
    • Zimmermann, H. (1992) 5′-nucleotidase: molecular structure and functional aspects. Biochem. J. 285, 345-365
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 2
    • 0034978361 scopus 로고    scopus 로고
    • Histamine increases interstitial adenosine concentration via activation of ecto-5′-nucleotidase in rat hearts in vivo
    • Obata, T., Kubota, S. and Yamanaka, Y. (2001) Histamine increases interstitial adenosine concentration via activation of ecto-5′-nucleotidase in rat hearts in vivo. J. Pharmacol. Exp. Ther. 298, 71-76
    • (2001) J. Pharmacol. Exp. Ther. , vol.298 , pp. 71-76
    • Obata, T.1    Kubota, S.2    Yamanaka, Y.3
  • 3
    • 0034522838 scopus 로고    scopus 로고
    • Nicorandil increases adenosine 5′-monophosphate-primed interstitial adenosine via activation of ecto-5′-nucleotidase in rat hearts
    • Sato, T., Obata, T., Yamanaka, Y. and Arita, M. (2000) Nicorandil increases adenosine 5′-monophosphate-primed interstitial adenosine via activation of ecto-5′-nucleotidase in rat hearts. Heart Vessels 15, 81-85
    • (2000) Heart Vessels , vol.15 , pp. 81-85
    • Sato, T.1    Obata, T.2    Yamanaka, Y.3    Arita, M.4
  • 4
    • 0032899717 scopus 로고    scopus 로고
    • Effect of salt loading on adenosine metabolism and receptor expression in renal cortex and medulla in rats
    • Zou, A. P., Wu, F., Li, P. L. and Cowley, Jr, A. W. (1999) Effect of salt loading on adenosine metabolism and receptor expression in renal cortex and medulla in rats. Hypertension 33, 511-516
    • (1999) Hypertension , vol.33 , pp. 511-516
    • Zou, A.P.1    Wu, F.2    Li, P.L.3    Cowley A.W., Jr.4
  • 6
    • 0025823076 scopus 로고
    • Synovial fluid 5′-nucleotidase activity. Relationship to other purine catabolic enzymes and to arthropathies associated with calcium crystal deposition
    • Wortmann, R. L., Veum, J. A. and Rachow, J. W. (1991) Synovial fluid 5′-nucleotidase activity. Relationship to other purine catabolic enzymes and to arthropathies associated with calcium crystal deposition. Arthritis Rheum. 34, 1014-1120
    • (1991) Arthritis Rheum. , vol.34 , pp. 1014-1120
    • Wortmann, R.L.1    Veum, J.A.2    Rachow, J.W.3
  • 8
    • 0032524568 scopus 로고    scopus 로고
    • Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′-nucleotidase by phospholipase C: Catalytic activation and modulation by the lipid bilayer
    • Letho, M. T. and Sharon, F. J. (1998) Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′-nucleotidase by phospholipase C: catalytic activation and modulation by the lipid bilayer. Biochem. J. 332, 101-109
    • (1998) Biochem. J. , vol.332 , pp. 101-109
    • Letho, M.T.1    Sharon, F.J.2
  • 10
    • 0031888647 scopus 로고    scopus 로고
    • Temperature effects on the structural and functional properties of GPI-anchored and anchor-less bull seminal plasma ecto-5′-nucleotidase
    • Fini, C., Coli, M., Floridi, A., D'Auria, S., Staiano, M., Nucci, R. and Rossi, M. (1998) Temperature effects on the structural and functional properties of GPI-anchored and anchor-less bull seminal plasma ecto-5′-nucleotidase. J. Biochem. 123, 269-274
    • (1998) J. Biochem. , vol.123 , pp. 269-274
    • Fini, C.1    Coli, M.2    Floridi, A.3    D'Auria, S.4    Staiano, M.5    Nucci, R.6    Rossi, M.7
  • 11
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 12
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg, A., Postel, W. and Gunther, S. (1988) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9, 531-546
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 13
    • 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
  • 14
    • 0023724982 scopus 로고
    • Isoelectric focusing in immobilized pH gradients with carrier ampholytes added for high-resolution phenotyping of bovine β-lactoglobulins: Characterization of a new genetic variant
    • Krause, I., Buchberger, J., Weiss, G., Pflugler, M. and Klostermeyer, H. (1988) Isoelectric focusing in immobilized pH gradients with carrier ampholytes added for high-resolution phenotyping of bovine β-lactoglobulins: characterization of a new genetic variant. Electrophoresis 9, 609-613
    • (1988) Electrophoresis , vol.9 , pp. 609-613
    • Krause, I.1    Buchberger, J.2    Weiss, G.3    Pflugler, M.4    Klostermeyer, H.5
  • 17
    • 0032544552 scopus 로고    scopus 로고
    • Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching
    • Damer, C., Partridge, J., Pearson, W. R. and Haystead, T. A. (1998) Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching. J. Biol. Chem. 273, 24396-24405
    • (1998) J. Biol. Chem. , vol.273 , pp. 24396-24405
    • Damer, C.1    Partridge, J.2    Pearson, W.R.3    Haystead, T.A.4
  • 18
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton, G. J. (1990) Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183, 403-428
    • (1990) Methods Enzymol. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 19
    • 0023571979 scopus 로고
    • Evaluation and improvements in the automatic alignment of protein sequences
    • Barton, G. J. and Sternberg, M. J. E. (1987) Evaluation and improvements in the automatic alignment of protein sequences. Protein Eng. 1, 89-94
    • (1987) Protein Eng. , vol.1 , pp. 89-94
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 20
    • 0032707718 scopus 로고    scopus 로고
    • Validation of nuclear magnetic resonance structures of proteins and nucleic acids: Hydrogen geometry and nomenclature
    • Doreleijers, J. F., Vriend, G., Raves, M. L. and Kaptein, R. (1999) Validation of nuclear magnetic resonance structures of proteins and nucleic acids: hydrogen geometry and nomenclature. Proteins: Struct. Funct. Genet. 37, 404-416
    • (1999) Proteins: Struct. Funct. Genet. , vol.37 , pp. 404-416
    • Doreleijers, J.F.1    Vriend, G.2    Raves, M.L.3    Kaptein, R.4
  • 21
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 22
    • 77956741418 scopus 로고
    • Urtraviolet spectra of proteins and amino acids
    • Anfinsen, Jr, C. B., Anson, M. L., Bailey, K. and Edsall, J. T., eds. Academic Press, New York and London
    • Wetlaufer, D. B. (1962) Urtraviolet spectra of proteins and amino acids. In Advances in Protein Chemistry, vol. 17 (Anfinsen, Jr, C. B., Anson, M. L., Bailey, K. and Edsall, J. T., eds.), pp. 304-383, Academic Press, New York and London
    • (1962) Advances in Protein Chemistry , vol.17 , pp. 304-383
    • Wetlaufer, D.B.1
  • 23
    • 0032838536 scopus 로고    scopus 로고
    • Application of ESI MS/MS and MALDI-TOF-MS to structural analysis of the glycosylphosphatidylinositol-anchored protein
    • Taguchi, R., Hamakawa, N., Maekawa, N. and Ikezawa, H. (1999) Application of ESI MS/MS and MALDI-TOF-MS to structural analysis of the glycosylphosphatidylinositol-anchored protein. J. Biochem. (Tokyo) 126, 421-429
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 421-429
    • Taguchi, R.1    Hamakawa, N.2    Maekawa, N.3    Ikezawa, H.4
  • 24
    • 0035170507 scopus 로고    scopus 로고
    • GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources
    • Cooper, C. A., Harrison, M. J., Wilkins, M. R. and Packer, N. H. (2001) GlycoSuiteDB: a new curated relational database of glycoprotein glycan structures and their biological sources. Nucleic Acids Res. 29, 332-335
    • (2001) Nucleic Acids Res. , vol.29 , pp. 332-335
    • Cooper, C.A.1    Harrison, M.J.2    Wilkins, M.R.3    Packer, N.H.4
  • 25
    • 0024458171 scopus 로고
    • Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin
    • Stochaj, U., Dieckhoff, J., Mollenhauer, J., Cramer, M. and Mannherz, H. G. (1989) Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin. Biochim. Biophys. Acta 992, 385-392
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 385-392
    • Stochaj, U.1    Dieckhoff, J.2    Mollenhauer, J.3    Cramer, M.4    Mannherz, H.G.5
  • 26
    • 0028181051 scopus 로고
    • Distribution of endogenous and exogenous 5′-nucleotidase in bovine spermatozoa
    • Schiemann, P. J., Aliante, M., Wennemuth, G., Fini, C. and Aumüller, G. (1994) Distribution of endogenous and exogenous 5′-nucleotidase in bovine spermatozoa. Histochemistry 101, 253-262
    • (1994) Histochemistry , vol.101 , pp. 253-262
    • Schiemann, P.J.1    Aliante, M.2    Wennemuth, G.3    Fini, C.4    Aumüller, G.5
  • 27
    • 0032915156 scopus 로고    scopus 로고
    • X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site
    • Knöfel, T. and Sträter, N. (1999) X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site. Nat. Struct. Biol. 6, 448-453
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 448-453
    • Knöfel, T.1    Sträter, N.2
  • 28
    • 0035946945 scopus 로고    scopus 로고
    • Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures
    • Knöfel, T. and Sträter, N. (2001) Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures. J. Mol. Biol. 309, 239-254
    • (2001) J. Mol. Biol. , vol.309 , pp. 239-254
    • Knöfel, T.1    Sträter, N.2
  • 29
    • 0035946952 scopus 로고    scopus 로고
    • E. coli 5′-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion
    • Knöfel, T. and Sträter, N. (2001) E. coli 5′-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion. J. Mol. Biol. 309, 255-266
    • (2001) J. Mol. Biol. , vol.309 , pp. 255-266
    • Knöfel, T.1    Sträter, N.2
  • 30
    • 0025216517 scopus 로고
    • 5′-nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein
    • Fini, C., Palmerini, C. A., Damiani, P., Stochaj, U., Mannherz, H. G. and Florid. A. (1990) 5′-nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein. Biochim. Biophys. Acta 1038, 18-22
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 18-22
    • Fini, C.1    Palmerini, C.A.2    Damiani, P.3    Stochaj, U.4    Mannherz, H.G.5    Florid, A.6


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