메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

A Method to Measure Hydrolytic Activity of Adenosinetriphosphatases (ATPases)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM DERIVATIVE; AMMONIUM MOLYBDATE; ANTIMONY TARTRATE; ASCORBIC ACID; MOLYBDENUM; PHOSPHATE; RECOMBINANT ENZYME; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SULFURIC ACID; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CATION;

EID: 84874590157     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058615     Document Type: Article
Times cited : (32)

References (46)
  • 1
    • 84954214416 scopus 로고    scopus 로고
    • Catalytic and transport mechanism of the Sarco-(Endo)Plasmic reticulum Ca2+-ATPase (SERCA)
    • In: Futai M, Wada Y, Kaplan JH, editors, Weinheim: Wiley-VCH
    • Inesi G, Toyoshima C (2004) Catalytic and transport mechanism of the Sarco-(Endo)Plasmic reticulum Ca2+-ATPase (SERCA). In: Futai M, Wada Y, Kaplan JH, editors. Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology. Weinheim: Wiley-VCH. pp. 63-87.
    • (2004) Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology , pp. 63-87
    • Inesi, G.1    Toyoshima, C.2
  • 3
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • Kaplan JH, (2002) Biochemistry of Na,K-ATPase. Annu Rev Biochem 71: 511-535.
    • (2002) Annu Rev Biochem , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 4
    • 0038621773 scopus 로고    scopus 로고
    • Structure and mechanism of Na,K-ATPase: Functional Sites and Their Interactions
    • Jørgensen PL, Hakansson KO, Karlish SJD, (2003) Structure and mechanism of Na,K-ATPase: Functional Sites and Their Interactions. Annu Rev Physiol 65: 817-849.
    • (2003) Annu Rev Physiol , vol.65 , pp. 817-849
    • Jørgensen, P.L.1    Hakansson, K.O.2    Karlish, S.J.D.3
  • 5
    • 0018401053 scopus 로고
    • Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum
    • De Meis L, Vianna AL, (1979) Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum. Annu Rev Biochem 48: 275-292.
    • (1979) Annu Rev Biochem , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.L.2
  • 6
    • 79960340059 scopus 로고    scopus 로고
    • Development of a flow method for the determination of phosphate in estuarine and freshwaters--comparison of flow cells in spectrophotometric sequential injection analysis
    • Mesquita RBR, Ferreira MTSOB, Tóth I V, Bordalo AA, McKelvie ID, et al. (2011) Development of a flow method for the determination of phosphate in estuarine and freshwaters--comparison of flow cells in spectrophotometric sequential injection analysis. Anal Chim Acta 701: 15-22.
    • (2011) Anal Chim Acta , vol.701 , pp. 15-22
    • Mesquita, R.B.R.1    Ferreira, M.T.S.O.B.2    Tóth, I.V.3    Bordalo, A.A.4    McKelvie, I.D.5
  • 7
    • 79751505074 scopus 로고    scopus 로고
    • Determination of dissolved reactive and dissolved total phosphorus in water extract of soils
    • Matula J, (2011) Determination of dissolved reactive and dissolved total phosphorus in water extract of soils. Plant Soil Environ 57: 1-6.
    • (2011) Plant Soil Environ , vol.57 , pp. 1-6
    • Matula, J.1
  • 8
    • 33749535118 scopus 로고
    • Determination of organic phosphorus compounds by phosphate analysis
    • Ernster L, Lindberg O, (1956) Determination of organic phosphorus compounds by phosphate analysis. Methods Biochem Anal 3: 1-22.
    • (1956) Methods Biochem Anal , vol.3 , pp. 1-22
    • Ernster, L.1    Lindberg, O.2
  • 9
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske CH, Subbarow Y, (1925) The colorimetric determination of phosphorus. J Biol Chem 66: 375-400.
    • (1925) J Biol Chem , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 10
    • 0038446566 scopus 로고
    • Sur une reaction pouvant servir on dosage coloimetrique du phospore dans le fontes, les aciers, etc
    • Osmond MF, (1887) Sur une reaction pouvant servir on dosage coloimetrique du phospore dans le fontes, les aciers, etc. Bull Soc Chim 47: 745-749.
    • (1887) Bull Soc Chim , vol.47 , pp. 745-749
    • Osmond, M.F.1
  • 11
    • 39149104788 scopus 로고
    • On the estimation of phosphorus in biological material
    • Taylor AE, Miller CW, (1914) On the estimation of phosphorus in biological material. J Biol Chem 18: 215-224.
    • (1914) J Biol Chem , vol.18 , pp. 215-224
    • Taylor, A.E.1    Miller, C.W.2
  • 12
    • 0000807711 scopus 로고
    • The determination of inorganic phosphate in the presence of labile phosphate esters
    • Lowry OH, Lopez JA, (1946) The determination of inorganic phosphate in the presence of labile phosphate esters. J Biol Chem 162: 421-428.
    • (1946) J Biol Chem , vol.162 , pp. 421-428
    • Lowry, O.H.1    Lopez, J.A.2
  • 14
    • 70449151077 scopus 로고
    • The determination of phosphorus and phosphatase with N-phenyl-p-phenylenediamine
    • Dryer RL, Tammes AR, Routh JI, (1957) The determination of phosphorus and phosphatase with N-phenyl-p-phenylenediamine. J Biol Chem 225: 177-183.
    • (1957) J Biol Chem , vol.225 , pp. 177-183
    • Dryer, R.L.1    Tammes, A.R.2    Routh, J.I.3
  • 15
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphorus
    • Taussky HH, Shorr E, (1953) A microcolorimetric method for the determination of inorganic phosphorus. J Biol Chem 202: 675-685.
    • (1953) J Biol Chem , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 16
    • 0344493938 scopus 로고    scopus 로고
    • A simplified method for inorganic phosphate determination and its application for phosphate analysis in enzyme assays
    • Katewa SD, Katyare SS, (2003) A simplified method for inorganic phosphate determination and its application for phosphate analysis in enzyme assays. Anal Biochem 323: 180-187.
    • (2003) Anal Biochem , vol.323 , pp. 180-187
    • Katewa, S.D.1    Katyare, S.S.2
  • 17
    • 0035210993 scopus 로고    scopus 로고
    • Rapid, sensitive, microscale determination of phosphate in water and soil
    • D'Angelo E, Crutchfield J, Vandiviere M, (2001) Rapid, sensitive, microscale determination of phosphate in water and soil. J Environ Qual 30: 2206-2209.
    • (2001) J Environ Qual , vol.30 , pp. 2206-2209
    • D'Angelo, E.1    Crutchfield, J.2    Vandiviere, M.3
  • 19
    • 0015441879 scopus 로고
    • Phase changes in the lipid moieties of sarcoplasmic reticulum membranes induced by temperature and protein conformational changes
    • Eletr S, Inesi G, (1972) Phase changes in the lipid moieties of sarcoplasmic reticulum membranes induced by temperature and protein conformational changes. Biochim Biophys Acta 290: 178-185.
    • (1972) Biochim Biophys Acta , vol.290 , pp. 178-185
    • Eletr, S.1    Inesi, G.2
  • 21
    • 0016367998 scopus 로고
    • Isolation of (Na+ plus K+)-ATPase
    • Jørgensen PL, (1974) Isolation of (Na+ plus K+)-ATPase. Methods Enzymol 32: 277-290.
    • (1974) Methods Enzymol , vol.32 , pp. 277-290
    • Jørgensen, P.L.1
  • 22
    • 68349095078 scopus 로고    scopus 로고
    • High-yield heterologous expression of wild type and mutant Ca2+ ATPase: Characterization of Ca2+ binding sites by charge transfer
    • Liu Y, Pilankatta R, Lewis D, Inesi G, Tadini-Buoninsegni F, et al. (2009) High-yield heterologous expression of wild type and mutant Ca2+ ATPase: Characterization of Ca2+ binding sites by charge transfer. J Mol Biol 391: 858-871.
    • (2009) J Mol Biol , vol.391 , pp. 858-871
    • Liu, Y.1    Pilankatta, R.2    Lewis, D.3    Inesi, G.4    Tadini-Buoninsegni, F.5
  • 25
    • 0025737973 scopus 로고
    • Inhibition of the Sarcoplasmic-Reticulum Ca2+ Transport Atpase by Thapsigargin at Subnanomolar Concentrations
    • Sagara Y, Inesi G, (1991) Inhibition of the Sarcoplasmic-Reticulum Ca2+ Transport Atpase by Thapsigargin at Subnanomolar Concentrations. J Biol Chem 266: 13503-13506.
    • (1991) J Biol Chem , vol.266 , pp. 13503-13506
    • Sagara, Y.1    Inesi, G.2
  • 26
    • 0026050850 scopus 로고
    • Thapsigargin Inhibits the Sarcoplasmic or Endoplasmic-Reticulum Ca-ATPase Family of Calcium Pumps
    • Lytton J, Westlin M, Hanley MR, (1991) Thapsigargin Inhibits the Sarcoplasmic or Endoplasmic-Reticulum Ca-ATPase Family of Calcium Pumps. J Biol Chem 266: 17067-17071.
    • (1991) J Biol Chem , vol.266 , pp. 17067-17071
    • Lytton, J.1    Westlin, M.2    Hanley, M.R.3
  • 27
    • 69549106325 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain
    • Ogawa H, Shinoda T, Cornelius F, Toyoshima C, (2009) Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Proc Natl Acad Sci U S A 106: 13742-13747.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13742-13747
    • Ogawa, H.1    Shinoda, T.2    Cornelius, F.3    Toyoshima, C.4
  • 28
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump
    • Møller J V, Olesen C, Winther AM, Nissen P (2010) The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump. Q Rev Biophys: 1-66.
    • (2010) Q Rev Biophys , pp. 1-66
    • Møller, J.V.1    Olesen, C.2    Winther, A.M.3    Nissen, P.4
  • 29
    • 33846006918 scopus 로고    scopus 로고
    • Pre-steady state electrogenic events of Ca2+/H+ exchange and transport by the Ca2+-ATPase
    • Tadini-Buoninsegni F, Bartolommei G, Moncelli MR, Guidelli R, Inesi G, (2006) Pre-steady state electrogenic events of Ca2+/H+ exchange and transport by the Ca2+-ATPase. J Biol Chem 281: 37720-37727.
    • (2006) J Biol Chem , vol.281 , pp. 37720-37727
    • Tadini-Buoninsegni, F.1    Bartolommei, G.2    Moncelli, M.R.3    Guidelli, R.4    Inesi, G.5
  • 30
    • 80055094200 scopus 로고    scopus 로고
    • The Ca2+-ATPase (SERCA1) is inhibited by 4-aminoquinoline derivatives through interference with catalytic activation by Ca2+, whereas the ATPase E2 state remains functional
    • Bartolommei G, Tadini-Buoninsegni F, Moncelli MR, Gemma S, Camodeca C, et al. (2011) The Ca2+-ATPase (SERCA1) is inhibited by 4-aminoquinoline derivatives through interference with catalytic activation by Ca2+, whereas the ATPase E2 state remains functional. J Biol Chem 286: 38383-38389.
    • (2011) J Biol Chem , vol.286 , pp. 38383-38389
    • Bartolommei, G.1    Tadini-Buoninsegni, F.2    Moncelli, M.R.3    Gemma, S.4    Camodeca, C.5
  • 31
    • 1542284630 scopus 로고    scopus 로고
    • Production and characterization of reduced NAADP (nicotinic acid-adenine dinucleotide phosphate)
    • Billington RA, Thuring JW, Conway SJ, Packman L, Holmes AB, et al. (2004) Production and characterization of reduced NAADP (nicotinic acid-adenine dinucleotide phosphate). Biochem J 378: 275-280.
    • (2004) Biochem J , vol.378 , pp. 275-280
    • Billington, R.A.1    Thuring, J.W.2    Conway, S.J.3    Packman, L.4    Holmes, A.B.5
  • 32
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud R, Kessel M, Beuron F, Steven AC, Maurizi MR, (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J Biol Chem 273: 12476-12481.
    • (1998) J Biol Chem , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 35
    • 70349785247 scopus 로고    scopus 로고
    • Investigation of electrogenic partial reactions in detergent-solubilized Na,K-ATPase
    • Habeck M, Cirri E, Katz A, Karlish SJ, Apell H-J, (2009) Investigation of electrogenic partial reactions in detergent-solubilized Na,K-ATPase. Biochemistry 48: 9147-9155.
    • (2009) Biochemistry , vol.48 , pp. 9147-9155
    • Habeck, M.1    Cirri, E.2    Katz, A.3    Karlish, S.J.4    Apell, H.-J.5
  • 36
    • 0016631203 scopus 로고
    • Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range
    • Hess HH, Derr JE, (1975) Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range. Anal Biochem 63: 607-613.
    • (1975) Anal Biochem , vol.63 , pp. 607-613
    • Hess, H.H.1    Derr, J.E.2
  • 37
    • 0014809293 scopus 로고
    • Determination of lipid phosphorus in the nanomolar range
    • Chalvardjian A, Rudnicki E, (1970) Determination of lipid phosphorus in the nanomolar range. Anal Biochem 36: 225-226.
    • (1970) Anal Biochem , vol.36 , pp. 225-226
    • Chalvardjian, A.1    Rudnicki, E.2
  • 39
    • 84870986351 scopus 로고    scopus 로고
    • Mimicking the Intramolecular Hydrogen Bond: Synthesis, Biological Evaluation, and Molecular Modeling of Benzoxazines and Quinazolines as Potential Antimalarial Agents
    • Gemma S, Camodeca C, Brindisi M, Brogi S, Kukreja G, et al. (2012) Mimicking the Intramolecular Hydrogen Bond: Synthesis, Biological Evaluation, and Molecular Modeling of Benzoxazines and Quinazolines as Potential Antimalarial Agents. J Med Chem 55: 10387-10404.
    • (2012) J Med Chem , vol.55 , pp. 10387-10404
    • Gemma, S.1    Camodeca, C.2    Brindisi, M.3    Brogi, S.4    Kukreja, G.5
  • 40
    • 1142310685 scopus 로고    scopus 로고
    • Time-resolved charge movements in the sarcoplasmatic reticulum Ca-ATPase
    • Peinelt C, Apell H-J, (2004) Time-resolved charge movements in the sarcoplasmatic reticulum Ca-ATPase. Biophys J 86: 815-824.
    • (2004) Biophys J , vol.86 , pp. 815-824
    • Peinelt, C.1    Apell, H.-J.2
  • 42
    • 77953810364 scopus 로고    scopus 로고
    • Investigation of the enzymatic activity of the Na+,K+-ATPase via isothermal titration microcalorimetry
    • Noske R, Cornelius F, Clarke RJ, (2010) Investigation of the enzymatic activity of the Na+,K+-ATPase via isothermal titration microcalorimetry. Biochim Biophys Acta 1797: 1540-1545.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1540-1545
    • Noske, R.1    Cornelius, F.2    Clarke, R.J.3
  • 43
    • 0034672118 scopus 로고    scopus 로고
    • Preparation of Na,K-ATPase specifically modified on the anti-fluorescein antibody-inaccessible site by fluorescein 5'-isothiocyanate
    • Lin SH, Faller LD, (2000) Preparation of Na,K-ATPase specifically modified on the anti-fluorescein antibody-inaccessible site by fluorescein 5'-isothiocyanate. Anal Biochem 287: 303-312.
    • (2000) Anal Biochem , vol.287 , pp. 303-312
    • Lin, S.H.1    Faller, L.D.2
  • 44
    • 0023819992 scopus 로고
    • Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation
    • Forbush B, (1988) Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation. J Biol Chem 263: 7961-7969.
    • (1988) J Biol Chem , vol.263 , pp. 7961-7969
    • Forbush, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.