메뉴 건너뛰기




Volumn 122, Issue 3, 1997, Pages 531-536

Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins

Author keywords

ADP ribosylation; Bacterial toxins; Small subunit; Soluble guanylate cyclase

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BACTERIAL TOXIN; BOTULINUM TOXIN; CARBON MONOXIDE; CHOLERA TOXIN; GUANYLATE CYCLASE; HEME; NITRIC OXIDE; PERTUSSIS TOXIN;

EID: 0030796164     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021785     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0022608859 scopus 로고
    • The purified alpha subunits of Go and Gi from bovine brain require beta gamma for association with phospholipid vesicles
    • Sternweis, P.C. (1986) The purified alpha subunits of Go and Gi from bovine brain require beta gamma for association with phospholipid vesicles. J. Biol. Chem. 261, 631-637
    • (1986) J. Biol. Chem. , vol.261 , pp. 631-637
    • Sternweis, P.C.1
  • 3
    • 0025609164 scopus 로고
    • Identification of sites for alkylation by N-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins
    • Hoshino, S., Kikkawa, S., Takahashi, K., Itoh, H., Kajiro, Y., Kawasaki, H., Suzuki, K., Katada, T., and Ui, M. (1990) Identification of sites for alkylation by N-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins. FEBS Lett. 276, 227-231
    • (1990) FEBS Lett. , vol.276 , pp. 227-231
    • Hoshino, S.1    Kikkawa, S.2    Takahashi, K.3    Itoh, H.4    Kajiro, Y.5    Kawasaki, H.6    Suzuki, K.7    Katada, T.8    Ui, M.9
  • 4
    • 0026014211 scopus 로고
    • Mono-ADP-ribosylation in brain: Purification and characterization of ADP-ribosyltransferases affecting actin from rat brain
    • Matsuyama, S. and Tsuyama, S. (1991) Mono-ADP-ribosylation in brain: Purification and characterization of ADP-ribosyltransferases affecting actin from rat brain. J. Neurochern. 57, 1380-1387
    • (1991) J. Neurochern. , vol.57 , pp. 1380-1387
    • Matsuyama, S.1    Tsuyama, S.2
  • 5
    • 0028822610 scopus 로고
    • ADP-ribosylation in adrenal glands: Purification and characterization of mono-ADP-ribosyltransferases and ADP-ribosylhydrolase affecting cytoskeletal actin
    • Fujita, H., Okamoto, H., and Tsuyama, S. (1995) ADP-ribosylation in adrenal glands: Purification and characterization of mono-ADP-ribosyltransferases and ADP-ribosylhydrolase affecting cytoskeletal actin. Int. J. Biochem. Cell Biol. 27, 1065-1078
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1065-1078
    • Fujita, H.1    Okamoto, H.2    Tsuyama, S.3
  • 6
    • 0343883763 scopus 로고
    • Mono-ADP-ribosylation of actin and GTP-binding protein in neurotransduction in rat brain
    • (Wegmann, R.J. and Wegmann, M.A., eds.) Peeters Press, Leuven
    • Tsuyama, S., Matsuyama, S., Fujita, H., Awa, T., and Takahashi, K.P. (1992) Mono-ADP-ribosylation of actin and GTP-binding protein in neurotransduction in rat brain in Recent Advances in Cellular and Molecular Biology (Wegmann, R.J. and Wegmann, M.A., eds.) Vol. 3, pp. 95-107, Peeters Press, Leuven
    • (1992) Recent Advances in Cellular and Molecular Biology , vol.3 , pp. 95-107
    • Tsuyama, S.1    Matsuyama, S.2    Fujita, H.3    Awa, T.4    Takahashi, K.P.5
  • 8
    • 0025162764 scopus 로고
    • Molecular cloning and expression of cDNAs coding for soluble guanylate cyclase from rat lung
    • Nakane, M., Arai, K., Saheki, S., Kuno, T., Buechler, W., and Murad, F. (1990) Molecular cloning and expression of cDNAs coding for soluble guanylate cyclase from rat lung. J. Biol. Chem. 265, 16841-16845
    • (1990) J. Biol. Chem. , vol.265 , pp. 16841-16845
    • Nakane, M.1    Arai, K.2    Saheki, S.3    Kuno, T.4    Buechler, W.5    Murad, F.6
  • 9
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of ferrous and ferric states
    • Stone, J.R. and Marletta, M.A. (1994) Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of ferrous and ferric states. Biochemistry 33, 5636-5640
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 10
    • 0028861061 scopus 로고
    • Heme stoichiometry of heterodimeric soluble guanylate cyclase
    • Stone, J.R. and Marletta, M.A. (1995) Heme stoichiometry of heterodimeric soluble guanylate cyclase. Biochemistry 34, 14668-14674
    • (1995) Biochemistry , vol.34 , pp. 14668-14674
    • Stone, J.R.1    Marletta, M.A.2
  • 11
    • 0006109789 scopus 로고
    • Activation of purified soluble guanylate cyclase by protoporphyrin IX
    • Ignarro, L.J., Wood, K.S., and Wolin, M.S. (1982) Activation of purified soluble guanylate cyclase by protoporphyrin IX. Proc. Natl. Acad. Sci. USA 79, 2870-2873
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2870-2873
    • Ignarro, L.J.1    Wood, K.S.2    Wolin, M.S.3
  • 12
    • 0022993474 scopus 로고
    • Activation of soluble guanylate cyclase by NO-hemoproteins involves NO-heme exchange
    • Ignarro, L.J., Adams, J.B., Horwitz, P.M., and Wood, K.S. (1986) Activation of soluble guanylate cyclase by NO-hemoproteins involves NO-heme exchange. J. Biol. Chem. 261, 4997-5002
    • (1986) J. Biol. Chem. , vol.261 , pp. 4997-5002
    • Ignarro, L.J.1    Adams, J.B.2    Horwitz, P.M.3    Wood, K.S.4
  • 13
    • 0030745411 scopus 로고    scopus 로고
    • Effects of GTP on bound nitric oxide of soluble guanylate cyclase probed by resonance Raman spectroscopy
    • in press
    • Tomita, T., Ogura, T., Tsuyama, S., Imai, Y., and Kitagawa, T. (1997) Effects of GTP on bound nitric oxide of soluble guanylate cyclase probed by resonance Raman spectroscopy. Biochemistry, in press
    • (1997) Biochemistry
    • Tomita, T.1    Ogura, T.2    Tsuyama, S.3    Imai, Y.4    Kitagawa, T.5
  • 14
    • 0020491331 scopus 로고
    • Guanylate cyclase from bovine lung: A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme
    • Wolin, M.S., Wood, K.S., and Ignarro, L.J. (1982) Guanylate cyclase from bovine lung: A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme. J. Biol. Chem. 257, 13312-13320
    • (1982) J. Biol. Chem. , vol.257 , pp. 13312-13320
    • Wolin, M.S.1    Wood, K.S.2    Ignarro, L.J.3
  • 15
    • 0017186630 scopus 로고
    • A rapid and sensitive assay method for protein kinase
    • Hung, K.-P. and Robinson, J.C. (1976) A rapid and sensitive assay method for protein kinase. Anal. Biochem. 72, 593-599
    • (1976) Anal. Biochem. , vol.72 , pp. 593-599
    • Hung, K.-P.1    Robinson, J.C.2
  • 16
    • 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
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0006739227 scopus 로고
    • A spectrophotometric method for the simultaneous determination of myoglobin and haemoglobin in extracts of human muscle
    • deDuve, C. (1948) A spectrophotometric method for the simultaneous determination of myoglobin and haemoglobin in extracts of human muscle. Acta Chem. Scand. 2, 264-289
    • (1948) Acta Chem. Scand. , vol.2 , pp. 264-289
    • DeDuve, C.1
  • 19
    • 0026735580 scopus 로고
    • Nitric oxide syntase is a cytochrome P-450 type hemoprotein
    • White, K.A. and Marletta, M.A. (1992) Nitric oxide syntase is a cytochrome P-450 type hemoprotein. Biochemistry 31, 6627-6631
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 20
    • 0020494044 scopus 로고
    • The separation of the heme and apoheme forms of soluble guanylate cyclase. Biochem
    • Gerzer, R., Radany, N.E., and Garbers, D.L. (1982) The separation of the heme and apoheme forms of soluble guanylate cyclase. Biochem. Biophys. Res. Commun. 108, 678-686
    • (1982) Biophys. Res. Commun. , vol.108 , pp. 678-686
    • Gerzer, R.1    Radany, N.E.2    Garbers, D.L.3
  • 21
    • 0024021150 scopus 로고
    • The three-dimensional structure of c-H-ras p21: Implications for oncogene and G protein studies
    • Jurnak, F. (1988) The three-dimensional structure of c-H-ras p21: implications for oncogene and G protein studies. Trends Biochem. Sci. 13, 195-198
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 195-198
    • Jurnak, F.1
  • 22
    • 0023761537 scopus 로고
    • The primary structure of the larger subunit of soluble guanylyl cyclase from bovine lung. Homology between the two subunits of the enzyme
    • Koesling, D., Herz, J., Gausepohl, H., Niroomand, F., Hinsch, K.-D., Mulsh, A., Bohme, E., Schultz, G., and Frank, R. (1988) The primary structure of the larger subunit of soluble guanylyl cyclase from bovine lung. Homology between the two subunits of the enzyme. FEBS Lett. 239, 29-34
    • (1988) FEBS Lett. , vol.239 , pp. 29-34
    • Koesling, D.1    Herz, J.2    Gausepohl, H.3    Niroomand, F.4    Hinsch, K.-D.5    Mulsh, A.6    Bohme, E.7    Schultz, G.8    Frank, R.9
  • 23
    • 0018654087 scopus 로고
    • Activation of adenylate cyclase by choleragen
    • Moss, J. and Vaughan, M. (1979) Activation of adenylate cyclase by choleragen. Annu. Rev. Biochem. 48, 581-600
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 581-600
    • Moss, J.1    Vaughan, M.2
  • 24
    • 0022347238 scopus 로고
    • Pertussis toxin-catalyzed ADP-ribosylation of transdusin cysteine 347 is the ADP-ribose acceptor site
    • West, R.E. Jr., Moss, J., Vaughan, M., Liu, T., and Liu, T.-Y. (1985) Pertussis toxin-catalyzed ADP-ribosylation of transdusin cysteine 347 is the ADP-ribose acceptor site. J. Biol. Chem. 260, 14428-14430
    • (1985) J. Biol. Chem. , vol.260 , pp. 14428-14430
    • West Jr., R.E.1    Moss, J.2    Vaughan, M.3    Liu, T.4    Liu, T.-Y.5
  • 25
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., Fujiwara, M., and Narumiya, S. (1989) Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 27
    • 0027954423 scopus 로고
    • Dominant negative mutants of nitric oxide-sensitive guanylyl cyclase
    • Yuen, P.S.T., Doolittle, L.K., and Garbers, D.L. (1994) Dominant negative mutants of nitric oxide-sensitive guanylyl cyclase. J. Biol. Chem. 269, 791-793
    • (1994) J. Biol. Chem. , vol.269 , pp. 791-793
    • Yuen, P.S.T.1    Doolittle, L.K.2    Garbers, D.L.3
  • 28
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.G. (1987) G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 29
    • 0029990994 scopus 로고    scopus 로고
    • Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMP signaling system
    • Ingi, T., Cheng, J., and Ronnett, G.V. (1996) Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMP signaling system. Neuron 16, 835-842
    • (1996) Neuron , vol.16 , pp. 835-842
    • Ingi, T.1    Cheng, J.2    Ronnett, G.V.3
  • 31
    • 0028679708 scopus 로고
    • GTP-binding proteins: Heterotrimeric G proteins
    • Pennington, S.R. (1994) GTP-binding proteins: Heterotrimeric G proteins. Protein Profile 1, 208-215
    • (1994) Protein Profile , vol.1 , pp. 208-215
    • Pennington, S.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.