메뉴 건너뛰기




Volumn 36, Issue 4, 1998, Pages 293-304

Evidence for voltage-sensitive reaction steps in the mechanism of the red beet plasma membrane H+-ATPase

Author keywords

ATPase mechanism; Beta vulgaris; Bioenergetics; Electrogenic H+ transport; P type ATPase; Transport reaction mechanism

Indexed keywords

BETA VULGARIS;

EID: 0032053703     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(98)80043-0     Document Type: Article
Times cited : (1)

References (41)
  • 1
    • 0027333424 scopus 로고
    • Signal transduction in guard cells
    • [1] Assmann S.M., Signal transduction in guard cells, Annu. Rev. Cell Biol. 9 (1993) 345-375.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 345-375
    • Assmann, S.M.1
  • 2
    • 0025344156 scopus 로고
    • A continuous fluorimetric assay for ATPase activity
    • [2] Banik B., Roy S., A continuous fluorimetric assay for ATPase activity, Biochem J. 266 (1990) 611-614.
    • (1990) Biochem J. , vol.266 , pp. 611-614
    • Banik, B.1    Roy, S.2
  • 3
    • 0000514423 scopus 로고
    • Nitrate storage and retrieval in Beta vulgaris: Effects of nitrate and chloride on proton gradients in tonoplast vesicles
    • [3] Blumwald E., Poole R.J., Nitrate storage and retrieval in Beta vulgaris: Effects of nitrate and chloride on proton gradients in tonoplast vesicles, Proc. Natl. Acad. Sci. USA. 82 (1985) 3683-3687.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3683-3687
    • Blumwald, E.1    Poole, R.J.2
  • 4
    • 0000937143 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • [4] Bradford M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1979) 243-254.
    • (1979) Anal. Biochem. , vol.72 , pp. 243-254
    • Bradford, M.M.1
  • 5
    • 0002386102 scopus 로고
    • Phosphorylation and dephosphorylation reactions of the red beet plasma membrane ATPase studied in the transient state
    • [5] Briskin D.P., Phosphorylation and dephosphorylation reactions of the red beet plasma membrane ATPase studied in the transient state, Plant Physiol. 88 (1988) 84-91.
    • (1988) Plant Physiol. , vol.88 , pp. 84-91
    • Briskin, D.P.1
  • 8
    • 4243107522 scopus 로고
    • Proton-coupled sugar and amino acid transporters in plants
    • [8] Bush D.R., Proton-coupled sugar and amino acid transporters in plants, Annu. Rev. Plant Physiol. Mol. Biol. 44 (1993) 513-542.
    • (1993) Annu. Rev. Plant Physiol. Mol. Biol. , vol.44 , pp. 513-542
    • Bush, D.R.1
  • 9
    • 0028140357 scopus 로고
    • P-type ATPases of eucaryotes and bacteria: Sequence analysis and construction of phylogenetic trees
    • [9] Fagan M.J., Saier Jr M.H., P-type ATPases of eucaryotes and bacteria: sequence analysis and construction of phylogenetic trees, J. Mol. Evol. 38 (1994) 57-99.
    • (1994) J. Mol. Evol. , vol.38 , pp. 57-99
    • Fagan, M.J.1    Saier M.H., Jr.2
  • 10
    • 0028851238 scopus 로고
    • + transport and ATPase activity in purified plasma membrane vesicles from maize (Zea mays L.) roots
    • + transport and ATPase activity in purified plasma membrane vesicles from maize (Zea mays L.) roots, J. Exp. Bot. 46 (1995) 1169-1176.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1169-1176
    • Faraday, C.D.1    Spanswick, R.M.2
  • 11
    • 0001243085 scopus 로고
    • Effect of vanadate, molybdate and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots
    • [11] Gallagher S.R., Leonard R.T., Effect of vanadate, molybdate and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots, Plant Physiol. 70 (1982) 1335-1340.
    • (1982) Plant Physiol. , vol.70 , pp. 1335-1340
    • Gallagher, S.R.1    Leonard, R.T.2
  • 12
    • 0023956531 scopus 로고
    • Pyridine nucleotide oxidation by a plasma membrane fraction from red beet (Beta vulgaris L.) storage tissue
    • [12] Giannini J.L., Briskin D.P., Pyridine nucleotide oxidation by a plasma membrane fraction from red beet (Beta vulgaris L.) storage tissue, Arch. Biochem. Biophys. 260 (1988) 653-660.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 653-660
    • Giannini, J.L.1    Briskin, D.P.2
  • 14
    • 0030051028 scopus 로고    scopus 로고
    • + pump current-voltage relationships at various transmembrane gradients of the pumped cations
    • + pump current-voltage relationships at various transmembrane gradients of the pumped cations, Biochim. Biophys. Acta 1278 (1996) 137-146.
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 137-146
    • Glitsch, H.G.1    Schwarz, W.2    Tappe, A.3
  • 15
    • 0025326935 scopus 로고
    • Occluded cations in active transport
    • [15] Glynn I.M., Karlish S.J.D., Occluded cations in active transport, Annu. Rev. Biochem. 59 (1990) 171-205.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 171-205
    • Glynn, I.M.1    Karlish, S.J.D.2
  • 17
    • 0010559433 scopus 로고
    • Reaction-kinetic analysis of current-voltage relationships for electrogenic pumps in neurospora and acetabularia
    • [17] Gradmann D., Hansen U.-P., Slayman C.L., Reaction-kinetic analysis of current-voltage relationships for electrogenic pumps in Neurospora and Acetabularia, Curr. Topics Membr. Transp. 16 (1982) 257-276.
    • (1982) Curr. Topics Membr. Transp. , vol.16 , pp. 257-276
    • Gradmann, D.1    Hansen, U.-P.2    Slayman, C.L.3
  • 19
    • 0019851576 scopus 로고
    • Interpretation of current-voltage relationships for 'active' ion transport systems: I. Steady-state reaction-kinetic analysis of class-I mechanisms
    • [19] Hansen U.-P., Gradmann D., Sanders D., Slayman C.L., Interpretation of current-voltage relationships for 'active' ion transport systems: I. Steady-state reaction-kinetic analysis of class-I mechanisms, J. Membr. Biol. 63 (1981) 165-190.
    • (1981) J. Membr. Biol. , vol.63 , pp. 165-190
    • Hansen, U.-P.1    Gradmann, D.2    Sanders, D.3    Slayman, C.L.4
  • 20
    • 0028058903 scopus 로고
    • Partial reactions of the Na,K-ATPase: Determination of rate constants
    • [20] Heyse S.I., I. Wuddel, H.-J. Apell, Stürmer W., Partial reactions of the Na,K-ATPase: determination of rate constants, J. Gen. Physiol. 104 (1994) 197-240.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 197-240
    • Heyse, S.I.1    Wuddel, I.2    Apell, H.-J.3    Stürmer, W.4
  • 22
    • 0015442483 scopus 로고
    • Studies concerning the possible reconstitution of an active cation pump across an artificial membrane
    • [22] Jain M.K., White F.P., Stickholm A., Williams E., Corders E.H., Studies concerning the possible reconstitution of an active cation pump across an artificial membrane, J. Membr. Biol. 8 (1972) 363-388.
    • (1972) J. Membr. Biol. , vol.8 , pp. 363-388
    • Jain, M.K.1    White, F.P.2    Stickholm, A.3    Williams, E.4    Corders, E.H.5
  • 23
    • 0029175265 scopus 로고
    • +-ATPase from higher plants: Functional reconstitution into liposomes and its regulation by phospholipids
    • +-ATPase from higher plants: functional reconstitution into liposomes and its regulation by phospholipids, Plant Sci. 111 (1995) 117-131.
    • (1995) Plant Sci. , vol.111 , pp. 117-131
    • Kasamo, K.1    Sakakibara, Y.2
  • 24
    • 0000466402 scopus 로고
    • The guard cell-environment connection
    • [24] Kearns E.V., Assmann S.M., The guard cell-environment connection, Plant Physiol. 102 (1993) 711-715.
    • (1993) Plant Physiol. , vol.102 , pp. 711-715
    • Kearns, E.V.1    Assmann, S.M.2
  • 25
    • 0019874032 scopus 로고
    • +)-ATPase from ox brain. II. Kinetic characterization of phosphointermediates
    • +)-ATPase from ox brain. II. Kinetic characterization of phosphointermediates, Biochim. Biophys. Acta 643 (1981) 463-482.
    • (1981) Biochim. Biophys. Acta , vol.643 , pp. 463-482
    • Klodos, I.1    Nørby, J.G.2    Plesner, I.W.3
  • 26
    • 0021121404 scopus 로고
    • Thermodynamic and kinetic properties of electrogenic ion pumps
    • [26] Läuger P., Thermodynamic and kinetic properties of electrogenic ion pumps, Biochim. Biophys. Acta 779 (1984) 307-341.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 307-341
    • Läuger, P.1
  • 27
    • 0004068805 scopus 로고
    • Sinauer Associates, Inc, Sunderland MA
    • [27] Läuger P., Electrogenic Ion Pumps, Sinauer Associates, Inc, Sunderland MA., 1991.
    • (1991) Electrogenic Ion Pumps
    • Läuger, P.1
  • 28
    • 0023673131 scopus 로고
    • The vacuolar ATPase, a proton pump controlled by a slip
    • W. Stein (ed.), Alan R. Liss, inc., New York
    • [28] Moriyama Y., Nelson N., The vacuolar ATPase, a proton pump controlled by a slip, in: W. Stein (ed.), The ion pumps:structure, function and regulation, Alan R. Liss, inc., New York, 1988, pp 387-394.
    • (1988) The Ion Pumps:structure, Function and Regulation , pp. 387-394
    • Moriyama, Y.1    Nelson, N.2
  • 30
    • 0001618819 scopus 로고
    • Density gradient localization of plasma membrane and tonoplast from storage tissue of growing and dormant red beet. Characterization of proton transport and ATPase in tonoplast vesicles
    • [30] Poole R.J., Briskin D.P., Kratky Z., Johnstone R.M., Density gradient localization of plasma membrane and tonoplast from storage tissue of growing and dormant red beet. Characterization of proton transport and ATPase in tonoplast vesicles, Plant Physiol. 74 (1984) 549-556.
    • (1984) Plant Physiol. , vol.74 , pp. 549-556
    • Poole, R.J.1    Briskin, D.P.2    Kratky, Z.3    Johnstone, R.M.4
  • 31
    • 0026911103 scopus 로고
    • The acid growth theory of auxin-induced cell elongation is alive and well
    • [31] Rayle D.L., Cleland R.E., The acid growth theory of auxin-induced cell elongation is alive and well, Plant Physiol. 99 (1992) 1271-1274.
    • (1992) Plant Physiol. , vol.99 , pp. 1271-1274
    • Rayle, D.L.1    Cleland, R.E.2
  • 33
    • 0002398729 scopus 로고
    • Structure and function of plasma membrane ATPase
    • [33] Serrano R., Structure and function of plasma membrane ATPase, Annu. Rev. Plant Physiol. Mol. Biol. 40 (1989) 61-94.
    • (1989) Annu. Rev. Plant Physiol. Mol. Biol. , vol.40 , pp. 61-94
    • Serrano, R.1
  • 35
    • 84989684554 scopus 로고
    • Reconstitution and rapid partial purification of the red beet plasma membrane ATPase
    • [35] Singh S.P., Kesav B.V.S., Briskin D.P., Reconstitution and rapid partial purification of the red beet plasma membrane ATPase, Physiol. Plant. 69 (1987) 617-626.
    • (1987) Physiol. Plant. , vol.69 , pp. 617-626
    • Singh, S.P.1    Kesav, B.V.S.2    Briskin, D.P.3
  • 36
    • 0022266608 scopus 로고
    • Steady-state analysis of an electroenzyme
    • [36] Slayman C.L., Sanders D., Steady-state analysis of an electroenzyme, Biochem. Soc. Symp. 50 (1984) 11-29.
    • (1984) Biochem. Soc. Symp. , vol.50 , pp. 11-29
    • Slayman, C.L.1    Sanders, D.2
  • 38
    • 0010592270 scopus 로고
    • The nature of proton translocating ATPases in maize roots
    • [38] Tu S.-I., Loper M.T., Brauer D., Hsu A.-F., The nature of proton translocating ATPases in maize roots, J. Plant Nutrition 15 (1992) 929-944.
    • (1992) J. Plant Nutrition , vol.15 , pp. 929-944
    • Tu, S.-I.1    Loper, M.T.2    Brauer, D.3    Hsu, A.-F.4
  • 40
    • 0029089396 scopus 로고
    • Electrogenicity of the sodium transport pathway in the Na,K-ATPase probed by charged-pulse experiments
    • [40] Wuddel I., Apell H.-J., Electrogenicity of the sodium transport pathway in the Na,K-ATPase probed by charged-pulse experiments, Biophys J. 69 (1995) 909-921.
    • (1995) Biophys J. , vol.69 , pp. 909-921
    • Wuddel, I.1    Apell, H.-J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.