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Volumn 6, Issue 3, 2002, Pages 209-216

Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes

Author keywords

Compatible solutes; Lactate dehydrogenase; Mannosylglycerate; Thermal stabilization

Indexed keywords

ASPERGILLUS NIGER;

EID: 0036599177     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s007920100236     Document Type: Article
Times cited : (158)

References (42)
  • 1
    • 0033733112 scopus 로고    scopus 로고
    • Dynamic and static light scattering and fluorescence studies of the interactions between lactate dehydrogenase and poly(ethyleneimine)
    • Andersson MM, Hatti-Kaul R (2000) Dynamic and static light scattering and fluorescence studies of the interactions between lactate dehydrogenase and poly(ethyleneimine). J Phys Chem B 104:3660-3667
    • (2000) J Phys Chem B , vol.104 , pp. 3660-3667
    • Andersson, M.M.1    Hatti-Kaul, R.2
  • 2
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • Arakawa T, Timasheff SN (1983) Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch Biochem Biophys 224:169-177
    • (1983) Arch Biochem Biophys , vol.224 , pp. 169-177
    • Arakawa, T.1    Timasheff, S.N.2
  • 3
    • 0029786721 scopus 로고    scopus 로고
    • Proteases and glycosyl hydrolases from hyperthermophilic microorganisms
    • Bauer MW, Halio SB, Kelly RM (1996) Proteases and glycosyl hydrolases from hyperthermophilic microorganisms. Adv Protein Chem 48:271-305
    • (1996) Adv Protein Chem , vol.48 , pp. 271-305
    • Bauer, M.W.1    Halio, S.B.2    Kelly, R.M.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein dye-binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein dye-binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0032586949 scopus 로고    scopus 로고
    • Role of Nγ-acetyldiaminobutyrate as an enzyme stabilizer and an intermediate in the biosynthesis of hydroxyectoine
    • Cánovas D, Borges N, Vargas C, Ventosa A, Nieto JJ, Santos H (1999) Role of Nγ-acetyldiaminobutyrate as an enzyme stabilizer and an intermediate in the biosynthesis of hydroxyectoine. Appl Environ Microbiol 65:3774-3779
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3774-3779
    • Cánovas, D.1    Borges, N.2    Vargas, C.3    Ventosa, A.4    Nieto, J.J.5    Santos, H.6
  • 8
    • 0001644688 scopus 로고
    • Comparison of solute-induced protein stabilization in aqueous solution and in the frozen and dried states
    • Carpenter JF, Crowe JH, Arakawa T (1990) Comparison of solute-induced protein stabilization in aqueous solution and in the frozen and dried states. J Dairy Sci 73:3627-3636
    • (1990) J Dairy Sci , vol.73 , pp. 3627-3636
    • Carpenter, J.F.1    Crowe, J.H.2    Arakawa, T.3
  • 9
    • 0027966149 scopus 로고
    • Occurrence and role of di-myo-inositol-1,1 -phosphate in Methanococcus igneus
    • Ciulla RA, Burggraf S, Stetter KO, Roberts MF (1994) Occurrence and role of di-myo-inositol-1,1 -phosphate in Methanococcus igneus. Appl Environ Microbiol 60:3660-3664
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3660-3664
    • Ciulla, R.A.1    Burggraf, S.2    Stetter, K.O.3    Roberts, M.F.4
  • 10
    • 0031613817 scopus 로고    scopus 로고
    • An overview of the role and diversity of compatible solutes in Bacteria and Archaea
    • da Costa MS, Santos H, Galinski EA (1998) An overview of the role and diversity of compatible solutes in Bacteria and Archaea. Adv Biochem Eng Biotechnol 61:117-153
    • (1998) Adv Biochem Eng Biotechnol , vol.61 , pp. 117-153
    • Da Costa, M.S.1    Santos, H.2    Galinski, E.A.3
  • 11
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 12
    • 0027303817 scopus 로고
    • Compatible solutes of halophilic eubacteria: Molecular principles, water-solute interaction, stress protection
    • Galinski EA (1993) Compatible solutes of halophilic eubacteria: molecular principles, water-solute interaction, stress protection. Experientia 49:487-496
    • (1993) Experientia , vol.49 , pp. 487-496
    • Galinski, E.A.1
  • 13
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel R, König H (1988) Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol Lett 49:75-79
    • (1988) FEMS Microbiol Lett , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 14
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro
    • Hottiger T, De Virgilio C, Hall MN, Boller T, Wiemken A (1994) The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro. Eur J Biochem 219:187-193
    • (1994) Eur J Biochem , vol.219 , pp. 187-193
    • Hottiger, T.1    De Virgilio, C.2    Hall, M.N.3    Boller, T.4    Wiemken, A.5
  • 15
    • 0017382705 scopus 로고
    • Differential scanning calorimetry of the thermal denaturation of lactate dehydrogenase
    • Jacobson AL, Braun H (1977) Differential scanning calorimetry of the thermal denaturation of lactate dehydrogenase. Biochim Biophys Acta 493:142-153
    • (1977) Biochim Biophys Acta , vol.493 , pp. 142-153
    • Jacobson, A.L.1    Braun, H.2
  • 16
    • 0014401636 scopus 로고
    • Molecular weight and quaternary structure of lactic dehydrogenase. 3. Comparative determination by sedimentation analysis, light scattering and osmosis
    • Jaenicke R, Knof S (1968) Molecular weight and quaternary structure of lactic dehydrogenase. 3. Comparative determination by sedimentation analysis, light scattering and osmosis. Eur J Biochem 4:157-163
    • (1968) Eur J Biochem , vol.4 , pp. 157-163
    • Jaenicke, R.1    Knof, S.2
  • 17
    • 0001667712 scopus 로고
    • Methanophosphagen: Unique cyclic pyrophosphate isolated from Methanobacterium thermoautotrophicum
    • USA
    • Kanodia S, Roberts MF (1983) Methanophosphagen: unique cyclic pyrophosphate isolated from Methanobacterium thermoautotrophicum. Proc Natl Acad Sci USA 80:5217-5221
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 5217-5221
    • Kanodia, S.1    Roberts, M.F.2
  • 18
    • 0033180252 scopus 로고    scopus 로고
    • Extrinsic protein stabilization by naturally occurring osmolytes β-hydroxyectoine and betaine
    • Knapp S, Landenstein R, Galinski EA (1999) Extrinsic protein stabilization by naturally occurring osmolytes β-hydroxyectoine and betaine. Extremophiles 3:191-198
    • (1999) Extremophiles , vol.3 , pp. 191-198
    • Knapp, S.1    Landenstein, R.2    Galinski, E.A.3
  • 19
    • 0031614960 scopus 로고    scopus 로고
    • Proteins from hyperthermophiles: Stability and enzymatic catalysis close to the boiling point of water
    • Ladenstein R, Antranikian G (1998) Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water. Adv Biochem Eng Biotechnol 61:37-85
    • (1998) Adv Biochem Eng Biotechnol , vol.61 , pp. 37-85
    • Ladenstein, R.1    Antranikian, G.2
  • 21
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert K, Galinski EA (1992) Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl Microbiol Biotechnol 37:61-65
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 22
    • 0028981456 scopus 로고
    • Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furiosus in response to salinity and temperature
    • Martins LO, Santos H (1995) Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furiosus in response to salinity and temperature. Appl Environ Microbiol 61:3299-3303
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3299-3303
    • Martins, L.O.1    Santos, H.2
  • 23
    • 0029838122 scopus 로고    scopus 로고
    • New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogales
    • Martins LO, Carreto LS, da Costa MS, Santos H (1996) New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogales. J Bacteriol 178:5644-5651
    • (1996) J Bacteriol , vol.178 , pp. 5644-5651
    • Martins, L.O.1    Carreto, L.S.2    Da Costa, M.S.3    Santos, H.4
  • 25
    • 0027903881 scopus 로고
    • The role of trehalose and other carbohydrates in biopreservation
    • Newman YM, Ring SG, Colaco C (1993) The role of trehalose and other carbohydrates in biopreservation. Biotechnol Genet Eng Rev 11:263-264
    • (1993) Biotechnol Genet Eng Rev , vol.11 , pp. 263-264
    • Newman, Y.M.1    Ring, S.G.2    Colaco, C.3
  • 26
    • 0029031690 scopus 로고
    • Compatible solutes in the thermophilic bacteria Rhodothermus marinus and "Thermus thermophilus"
    • Nunes OC, Manaia CM, da Costa MS, Santos H (1995) Compatible solutes in the thermophilic bacteria Rhodothermus marinus and "Thermus thermophilus". Appl Environ Microbiol 61:2351-2357
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2351-2357
    • Nunes, O.C.1    Manaia, C.M.2    Da Costa, M.S.3    Santos, H.4
  • 27
    • 0030309476 scopus 로고    scopus 로고
    • Biotechnological applications of the disaccharide trehalose
    • Paiva CLA, Panek AD (1996) Biotechnological applications of the disaccharide trehalose. Biotechnol Ann Rev 2:293-314
    • (1996) Biotechnol Ann Rev , vol.2 , pp. 293-314
    • Paiva, C.L.A.1    Panek, A.D.2
  • 28
    • 0028173327 scopus 로고
    • A prominent role for glucosylglycerol in the adaptation of Pseudomonas mendocina SKB70 to osmotic stress
    • Pocard JA, Smith LT, Smith GM, Le Rudulier D (1994) A prominent role for glucosylglycerol in the adaptation of Pseudomonas mendocina SKB70 to osmotic stress. J Bacteriol 176:6877-6884
    • (1994) J Bacteriol , vol.176 , pp. 6877-6884
    • Pocard, J.A.1    Smith, L.T.2    Smith, G.M.3    Le Rudulier, D.4
  • 29
    • 0031031303 scopus 로고    scopus 로고
    • Characterization of di-myo-inositol-1,1 -phosphate in the hyperthermophilic bacterium Thermotoga maritima
    • Ramakrishnan V, Verhagen MFJM, Adams MWW (1997) Characterization of di-myo-inositol-1,1 -phosphate in the hyperthermophilic bacterium Thermotoga maritima. Appl Environ Microbiol 63:347-350
    • (1997) Appl Environ Microbiol , vol.63 , pp. 347-350
    • Ramakrishnan, V.1    Verhagen, M.F.J.M.2    Adams, M.W.W.3
  • 31
    • 0031036609 scopus 로고    scopus 로고
    • Development of a defined and minimal media for the growth of the hyperthermophilic archaeon Pyrococcus furiosus Vc1
    • Raven NDH, Sharp RJ (1997) Development of a defined and minimal media for the growth of the hyperthermophilic archaeon Pyrococcus furiosus Vc1. FEMS Microbiol Lett 146:135-141
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 135-141
    • Raven, N.D.H.1    Sharp, R.J.2
  • 33
    • 0034981263 scopus 로고    scopus 로고
    • Organic solutes from thermophiles and hyperthermophiles
    • Santos H, da Costa MS (2001) Organic solutes from thermophiles and hyperthermophiles. Methods Enzymol 336:302-315
    • (2001) Methods Enzymol , vol.336 , pp. 302-315
    • Santos, H.1    Da Costa, M.S.2
  • 34
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1 -phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz S, Sonnenbichler J, Schäfer W, Hensel R (1992) Di-myo-inositol-1,1 -phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett 306:239-242
    • (1992) FEBS Lett , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schäfer, W.3    Hensel, R.4
  • 35
    • 0031785262 scopus 로고    scopus 로고
    • Activation and thermostabilization effects of cyclic 2,3- diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri
    • Shima S, Hérault DA, Berkessel A, Thauer RK (1998) Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri. Arch Microbiol 170:469-472
    • (1998) Arch Microbiol , vol.170 , pp. 469-472
    • Shima, S.1    Hérault, D.A.2    Berkessel, A.3    Thauer, R.K.4
  • 36
    • 0033136552 scopus 로고    scopus 로고
    • Combined effect of the growth temperature and salinity of the medium on the accumulation of compatible solutes by Rhodothermus marinus and Rhodothermus obamensis
    • Silva Z, Borges N, Martins LO, Wait R, da Costa MS, Santos H (1999) Combined effect of the growth temperature and salinity of the medium on the accumulation of compatible solutes by Rhodothermus marinus and Rhodothermus obamensis. Extremophiles 3:163-172
    • (1999) Extremophiles , vol.3 , pp. 163-172
    • Silva, Z.1    Borges, N.2    Martins, L.O.3    Wait, R.4    Da Costa, M.S.5    Santos, H.6
  • 37
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer MA, Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1:639-648
    • (1998) Mol Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 38
    • 0024043207 scopus 로고
    • Osmotic control of glycine betaine biosynthesis and degradation in Rhizobium meliloti
    • Smith LT, Pocard JA, Bernard T, Le Rudulier D (1988) Osmotic control of glycine betaine biosynthesis and degradation in Rhizobium meliloti. J Bacteriol 170:3142-3149
    • (1988) J Bacteriol , vol.170 , pp. 3142-3149
    • Smith, L.T.1    Pocard, J.A.2    Bernard, T.3    Le Rudulier, D.4
  • 39
    • 0014684343 scopus 로고
    • Heterogeneity of presumably homogeneous protein preparations
    • Susor WA, Kochman M, Rutter WJ (1969) Heterogeneity of presumably homogeneous protein preparations. Science 165:1260-1262
    • (1969) Science , vol.165 , pp. 1260-1262
    • Susor, W.A.1    Kochman, M.2    Rutter, W.J.3
  • 40
    • 0000191753 scopus 로고
    • Lactate dehydrogenase. UV method with pyruvate and NADH
    • Bergmeyer HU (ed), 3rd edn. VCH, Weinheim
    • Vassault A (1987) Lactate dehydrogenase. UV method with pyruvate and NADH. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 3, 3rd edn. VCH, Weinheim, pp 118-126
    • (1987) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1
  • 42
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-β aggregation pathway with chemical chaperones
    • Yang DS, Yip CM, Huang THJ, Chakrabartty A, Fraser PE (1999) Manipulating the amyloid-β aggregation pathway with chemical chaperones. J Biol Chem 274:32970-32974
    • (1999) J Biol Chem , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.J.3    Chakrabartty, A.4    Fraser, P.E.5


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