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Volumn 5, Issue 1, 2003, Pages 108-115

Measuring solution viscosity and its effect on enzyme activity

Author keywords

Trelahose; Viscosity

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLYCEROL; PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SOLVENT; SUCROSE; TREHALOSE;

EID: 0347930808     PISSN: 14809222     EISSN: None     Source Type: Journal    
DOI: 10.1251/bpo52     Document Type: Article
Times cited : (105)

References (20)
  • 1
    • 0345583701 scopus 로고    scopus 로고
    • Protein folding as a diffusional process
    • Jacob M, Schmid FX. Protein folding as a diffusional process. Biochemistry 1999; 38:13773-13779.
    • (1999) Biochemistry , vol.38 , pp. 13773-13779
    • Jacob, M.1    Schmid, F.X.2
  • 2
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers HA. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 1940; 7:284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 4
    • 0024463170 scopus 로고
    • Kinetics of the lactate dehydrogenase reaction in high-viscosity media
    • Demchenko AP, Ruskyn OI, Saburova EA. Kinetics of the lactate dehydrogenase reaction in high-viscosity media. Biochim Biophys Acta 1989; 998: 196-203.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 196-203
    • Demchenko, A.P.1    Ruskyn, O.I.2    Saburova, E.A.3
  • 7
    • 0034717064 scopus 로고    scopus 로고
    • Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: The flavodoxin story
    • van Mierlo CP, Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J Biotechnol 2000; 79:281-298.
    • (2000) J. Biotechnol. , vol.79 , pp. 281-298
    • van Mierlo, C.P.1    Steensma, E.2
  • 8
    • 0031889847 scopus 로고    scopus 로고
    • A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass
    • Cordone L, Galajda P, Vitrano E, Gassmann A, Ostermann A, Parak F. A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass. Eur Biophys J 1998; 27:173-176.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 173-176
    • Cordone, L.1    Galajda, P.2    Vitrano, E.3    Gassmann, A.4    Ostermann, A.5    Parak, F.6
  • 9
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima C, Takasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 2000; 405:647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Takasako, M.2    Nomura, H.3    Ogawa, H.4
  • 11
    • 0036334644 scopus 로고    scopus 로고
    • +-ATPase from Kluyveromyces lactis: Dependence on viscosity and temperature
    • +-ATPase from Kluyveromyces lactis: dependence on viscosity and temperature. J Bacteriol 2002; 184:4384-4391.
    • (2002) J. Bacteriol. , vol.184 , pp. 4384-4391
    • Sampedro, J.G.1    Muñoz-Clares, R.A.2    Uribe, S.3
  • 12
    • 0018380431 scopus 로고
    • The effects of vanadate on the plasma membrane ATPase of Neurospora crassa
    • Bowman BJ, Slayman CW. The effects of vanadate on the plasma membrane ATPase of Neurospora crassa. J Biol Chem 1979; 254:2928-2934.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2928-2934
    • Bowman, B.J.1    Slayman, C.W.2
  • 15
    • 0021100407 scopus 로고
    • Alterations in the structure of the ribose moiety of ATP reduce its effectiveness as a substrate for the sarcoplasmic reticulum ATPase
    • Anderson KW, Murphy AJ. Alterations in the structure of the ribose moiety of ATP reduce its effectiveness as a substrate for the sarcoplasmic reticulum ATPase. J Biol Chem 1983; 258:14276-14278.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14276-14278
    • Anderson, K.W.1    Murphy, A.J.2
  • 16
    • 0034613031 scopus 로고    scopus 로고
    • c,T-dependence of the viscosity and the self-diffusion coefficients in some aqueous carbohydrate solutions
    • Rampp M, Buttersack C, Ludemann HD. c,T-dependence of the viscosity and the self-diffusion coefficients in some aqueous carbohydrate solutions. Carbohydr Res 2000; 328:561-572.
    • (2000) Carbohydr. Res. , vol.328 , pp. 561-572
    • Rampp, M.1    Buttersack, C.2    Ludemann, H.D.3
  • 17
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: A water effect on hemoglobin
    • Colombo MF, Rau DC, Parsegian A. Protein solvation in allosteric regulation:a water effect on hemoglobin. Science 1992; 256:655-659.
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, A.3
  • 18
    • 0025174784 scopus 로고
    • Fumarase: Viscosity dependence of the kinetics parameters
    • Sweet W, Blanchard JS. Fumarase:viscosity dependence of the kinetics parameters. Arch Biochem Biophys 1990; 277:196-202.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 196-202
    • Sweet, W.1    Blanchard, J.S.2
  • 19
    • 0023234281 scopus 로고
    • Enzyme kinetics in solvent of increased viscosity. Dynamic aspects of carbonic anhydrase catalysis
    • Pocker Y, Janjic N. Enzyme kinetics in solvent of increased viscosity. Dynamic aspects of carbonic anhydrase catalysis. Biochemistry 1990; 26:2597-2606.
    • (1990) Biochemistry , vol.26 , pp. 2597-2606
    • Pocker, Y.1    Janjic, N.2
  • 20
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do these solvents affects these process
    • Timasheff SN. The control of protein stability and association by weak interactions with water: How do these solvents affects these process. Annu Rev Biophys Biomol Struct 1993; 22:67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.