메뉴 건너뛰기




Volumn 1656, Issue 2-3, 2004, Pages 88-95

Thermoinactivaion analysis of vacuolar H+-pyrophosphatase

Author keywords

Circular dichroism; Differential scanning calorimetry; differential scanning calorimetry; DSC; FITC; fluorescein 5 isothiocyanate; PPase; pyrophosphatase; Subunit interaction; Thermoinactivation; Tonoplast; Vacuolar H+ pyrophosphatase

Indexed keywords

CARRIER PROTEIN; FLUORESCEIN ISOTHIOCYANATE; HYDROGEN; INORGANIC PYROPHOSPHATASE; LIGAND; ENZYME INHIBITOR; PROTEIN SUBUNIT; PROTON;

EID: 3142657551     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.02.001     Document Type: Article
Times cited : (8)

References (32)
  • 5
    • 0002900649 scopus 로고
    • +-translocating inorganic pyrophosphatases from vacuole membranes of red beet
    • +-translocating inorganic pyrophosphatases from vacuole membranes of red beet. Plant Physiol. 91:1989;34-38
    • (1989) Plant Physiol. , vol.91 , pp. 34-38
    • Sarafian, V.1    Poole, R.J.2
  • 6
    • 0024306480 scopus 로고
    • Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean
    • Maeshima M., Yoshida S. Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean. J. Biol. Chem. 264:1989;20068-20073
    • (1989) J. Biol. Chem. , vol.264 , pp. 20068-20073
    • Maeshima, M.1    Yoshida, S.2
  • 8
    • 0000127303 scopus 로고
    • An essential arginyl residue in the tonoplst pyrophosphatase from etiolated mung bean seedlings
    • Kuo S.Y., Pan R.L. An essential arginyl residue in the tonoplst pyrophosphatase from etiolated mung bean seedlings. Plant Physiol. 93:1990;1128-1133
    • (1990) Plant Physiol. , vol.93 , pp. 1128-1133
    • Kuo, S.Y.1    Pan, R.L.2
  • 10
    • 0030868387 scopus 로고    scopus 로고
    • +-pyrophosphatase by N,N′- dicyclohexylcarbodiimide
    • +-pyrophosphatase by N, N′-dicyclohexylcarbodiimide. J. Biol. Chem. 272:1997;22340-22348
    • (1997) J. Biol. Chem. , vol.272 , pp. 22340-22348
    • Zhen, R.-G.1    Kim, E.J.2    Rea, P.A.3
  • 18
    • 0029915379 scopus 로고    scopus 로고
    • Structural stability of chloroplast coupling factor 1 determined by differential scanning calorimetry and cold inactivation
    • Hightower K.E., McCarty R.E. Structural stability of chloroplast coupling factor 1 determined by differential scanning calorimetry and cold inactivation. Biochemistry. 35:1996;4852-4857
    • (1996) Biochemistry , vol.35 , pp. 4852-4857
    • Hightower, K.E.1    McCarty, R.E.2
  • 20
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts J.F., Lin L.N. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry. 29:1990;6927-6940
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 21
    • 0023709866 scopus 로고
    • Analysis of processes causing thermal inactivation of enzymes
    • Ahern T.J., Klibanov A.M. Analysis of processes causing thermal inactivation of enzymes. Methods Biochem. Anal. 33:1988;91-127
    • (1988) Methods Biochem. Anal. , vol.33 , pp. 91-127
    • Ahern, T.J.1    Klibanov, A.M.2
  • 22
    • 0025094316 scopus 로고
    • Irreversible thermoinactivation of glucoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groups
    • Munch O., Tritsch D. Irreversible thermoinactivation of glucoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groups. Biochim. Biophys. Acta. 1041:1990;111-116
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 111-116
    • Munch, O.1    Tritsch, D.2
  • 23
    • 0031042332 scopus 로고    scopus 로고
    • Kinetic and thermodynamic thermal stabilities of ribonuclease a and ribonuclease B
    • Arnold U., Ulbrich-Hofmann R. Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B. Biochemistry. 36:1997;2166-2172
    • (1997) Biochemistry , vol.36 , pp. 2166-2172
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 24
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorous
    • Fiske C.H., Subbarow Y. The colorimetric determination of phosphorous. J. Biol. Chem. 66:1925;378-400
    • (1925) J. Biol. Chem. , vol.66 , pp. 378-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 26
    • 0022485196 scopus 로고
    • Artificial reductant enhancement of the Lowry method for protein determination
    • Larson E., Howlett B., Jagendorf A.T. Artificial reductant enhancement of the Lowry method for protein determination. Anal. Biochem. 155:1986;243-248
    • (1986) Anal. Biochem. , vol.155 , pp. 243-248
    • Larson, E.1    Howlett, B.2    Jagendorf, A.T.3
  • 27
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.H. Rapid and sensitive method for the microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.H.1
  • 28
    • 0026253633 scopus 로고
    • The helix-coil transition in heterogeneous peptides with specific side-chain interactions: Theory and comparison with CD spectral data
    • Gans P.J., Lyu P.C., Manning M.C., Woody R.W., Kallenbach N.R. The helix-coil transition in heterogeneous peptides with specific side-chain interactions: theory and comparison with CD spectral data. Biopolymers. 31:1991;1605-1614
    • (1991) Biopolymers , vol.31 , pp. 1605-1614
    • Gans, P.J.1    Lyu, P.C.2    Manning, M.C.3    Woody, R.W.4    Kallenbach, N.R.5
  • 29
    • 0242416537 scopus 로고    scopus 로고
    • Hydrodynamic and spectroscopic studies of substrate binding to human recombinant deoxycytidine kinase
    • Mani R.S., Usova E.V., Eriksson S., Cass C.E. Hydrodynamic and spectroscopic studies of substrate binding to human recombinant deoxycytidine kinase. Nucleosides Nucleotides Nucleic Acids. 22:2003;175-192
    • (2003) Nucleosides Nucleotides Nucleic Acids , vol.22 , pp. 175-192
    • Mani, R.S.1    Usova, E.V.2    Eriksson, S.3    Cass, C.E.4
  • 30
    • 0026052762 scopus 로고
    • Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase
    • Morin P.E., Freire E. Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase. Biochemistry. 30:1991;8494-8500
    • (1991) Biochemistry , vol.30 , pp. 8494-8500
    • Morin, P.E.1    Freire, E.2
  • 31
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics
    • Waldron T.T., Murphy K.P. Stabilization of proteins by ligand binding: application to drug screening and determination of unfolding energetics. Biochemistry. 42:2003;5058-5064
    • (2003) Biochemistry , vol.42 , pp. 5058-5064
    • Waldron, T.T.1    Murphy, K.P.2
  • 32
    • 0024977948 scopus 로고
    • Cold inactivation of vacuolar proton-ATPases
    • Moriyama Y., Nelson N. Cold inactivation of vacuolar proton-ATPases. J. Biol. Chem. 264:1989;3577-3582
    • (1989) J. Biol. Chem. , vol.264 , pp. 3577-3582
    • Moriyama, Y.1    Nelson, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.