메뉴 건너뛰기




Volumn 74, Issue 5, 1998, Pages 2666-2673

Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: A test of the counteraction hypothesis

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE; MUSCLE ENZYME; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRIMETHYLAMINE OXIDE; UREA;

EID: 0031967834     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77972-X     Document Type: Article
Times cited : (131)

References (53)
  • 1
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T., and S. N. Timasheff. 1982. Stabilization of protein structure by sugars. Biochemistry. 21:6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 2
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • Arakawa, T., and S. N. Timasheff. 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
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T., and S. N. Timasheff. 1985. The stabilization of proteins by osmolytes. Biophys. J. 47:411-414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 4
    • 0023030796 scopus 로고
    • Predominant osmotically active organic solutes in rat and rabbit renal medullas
    • Bagnasco, S., R. Balaban, H. M. Fales, Y.-M. Yang, and M. Burg. 1986. Predominant osmotically active organic solutes in rat and rabbit renal medullas. J. Biol. Chem. 261:5872-5877.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5872-5877
    • Bagnasco, S.1    Balaban, R.2    Fales, H.M.3    Yang, Y.-M.4    Burg, M.5
  • 5
    • 0014601044 scopus 로고
    • Kinetic properties of adenosine deaminase in mixed aqueous solvents
    • Bolen, D. W., and J. R. Fisher. 1969. Kinetic properties of adenosine deaminase in mixed aqueous solvents. Biochemistry. 8:4239-4246.
    • (1969) Biochemistry , vol.8 , pp. 4239-4246
    • Bolen, D.W.1    Fisher, J.R.2
  • 6
    • 0011190548 scopus 로고
    • Glycerol and other carbohydrate osmotic effectors
    • Springer-Verlag, Berlin, Heidelberg
    • Borowitzka, L. J. 1985. Glycerol and other carbohydrate osmotic effectors. In Transport Processes, Iono-and Osmoregulation. Springer-Verlag, Berlin, Heidelberg. 437-453.
    • (1985) Transport Processes, Iono- and Osmoregulation , pp. 437-453
    • Borowitzka, L.J.1
  • 7
    • 0015966621 scopus 로고
    • The salt relations of marine and halophilic species of the unicellular green alga, Dunaliella: The role of glycerol as a compatible solute
    • Borowitzka, L. J., and A. D. Brown. 1974. The salt relations of marine and halophilic species of the unicellular green alga, Dunaliella: the role of glycerol as a compatible solute. Arch. Microbiol. 96:37-52.
    • (1974) Arch. Microbiol. , vol.96 , pp. 37-52
    • Borowitzka, L.J.1    Brown, A.D.2
  • 8
    • 0018474573 scopus 로고
    • Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates
    • Bowlus, R. D., and G. N. Somero. 1979. Solute compatibility with enzyme function and structure: rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates. J. Exp. Zool. 208:137-151.
    • (1979) J. Exp. Zool. , vol.208 , pp. 137-151
    • Bowlus, R.D.1    Somero, G.N.2
  • 9
    • 0017474382 scopus 로고
    • Free amino acids in tissues of the skate Raja erinacea and the stingray Dasvatis sabina: Effects of environmental dilution
    • Boyd, T. A., C.-J. Cha, R. P. Forster, and L. Goldstein. 1977. Free amino acids in tissues of the skate Raja erinacea and the stingray Dasvatis sabina: effects of environmental dilution. J. Exp. Zool. 199:435-442.
    • (1977) J. Exp. Zool. , vol.199 , pp. 435-442
    • Boyd, T.A.1    Cha, C.-J.2    Forster, R.P.3    Goldstein, L.4
  • 10
    • 0015406621 scopus 로고
    • Water relations of sugar-tolerant yeasts: The role of intracellular polyols
    • Brown, A. D., and J. R. Simpson. 1972. Water relations of sugar-tolerant yeasts: the role of intracellular polyols. J. Gen. Microbiol. 72:589-591.
    • (1972) J. Gen. Microbiol. , vol.72 , pp. 589-591
    • Brown, A.D.1    Simpson, J.R.2
  • 11
    • 0029987341 scopus 로고    scopus 로고
    • Glycerophosphocholine and betaine counteract the effect of urea on pyruvate kinase
    • Burg, M. B., E. D. Kwon, and E. M. Peters. 1996. Glycerophosphocholine and betaine counteract the effect of urea on pyruvate kinase. Kidney Int. 50:S1-S5.
    • (1996) Kidney Int. , vol.50
    • Burg, M.B.1    Kwon, E.D.2    Peters, E.M.3
  • 12
    • 0031427001 scopus 로고    scopus 로고
    • Urea and methylamines have similar effects on aldose reductase activity
    • Burg, M. B., and E. M. Peters. 1997. Urea and methylamines have similar effects on aldose reductase activity. Am. J. Physiol. Renal Physiol. 42:F1048-F1053.
    • (1997) Am. J. Physiol. Renal Physiol. , vol.42
    • Burg, M.B.1    Peters, E.M.2
  • 13
    • 0015919599 scopus 로고
    • Factors affecting tetramer dissociation of rabbit muscle lactate dehydrogenase and reactivity of its sulfhydryl groups
    • Cho, I. C., and H. Swaisgood. 1973. Factors affecting tetramer dissociation of rabbit muscle lactate dehydrogenase and reactivity of its sulfhydryl groups. Biochemistry. 12:1572-1577.
    • (1973) Biochemistry , vol.12 , pp. 1572-1577
    • Cho, I.C.1    Swaisgood, H.2
  • 14
    • 0023925884 scopus 로고
    • i of the calcium-ATPase of sarcoplasmic reticulum
    • i of the calcium-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 263:157-161.
    • (1988) J. Biol. Chem. , vol.263 , pp. 157-161
    • De Meis, L.1
  • 15
    • 0014933421 scopus 로고
    • Physiological concentrations of lactate dehydrogenases and substrate inhibition
    • Everse, J., R. L. Berger, and N. O. Kaplan. 1970. Physiological concentrations of lactate dehydrogenases and substrate inhibition. Science. 168:1236-1238.
    • (1970) Science , vol.168 , pp. 1236-1238
    • Everse, J.1    Berger, R.L.2    Kaplan, N.O.3
  • 17
    • 0017163943 scopus 로고
    • Intracellular osmoregulatory role of amino acids and urea in marine elasmobranchs
    • Forster, R. P., and L. Goldstein. 1976. Intracellular osmoregulatory role of amino acids and urea in marine elasmobranchs. Am. J. Physiol. 230: 925-931.
    • (1976) Am. J. Physiol. , vol.230 , pp. 925-931
    • Forster, R.P.1    Goldstein, L.2
  • 18
    • 0001644129 scopus 로고
    • Determination of dissociation constants of coenzymes and abortive ternary complexes with rabbit muscle lactate dehydrogenase from fluorescence measurements
    • Fromm, H. J. 1963. Determination of dissociation constants of coenzymes and abortive ternary complexes with rabbit muscle lactate dehydrogenase from fluorescence measurements. J. Biol. Chem. 238:2938-2944.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2938-2944
    • Fromm, H.J.1
  • 19
    • 0025666432 scopus 로고
    • Importance of organic osmolytes for osmoregulattion by renal medullary cells
    • Garcia-Perez, A., and M. B. Burg. 1990. Importance of organic osmolytes for osmoregulattion by renal medullary cells. Hypertension. 16:595-602.
    • (1990) Hypertension , vol.16 , pp. 595-602
    • Garcia-Perez, A.1    Burg, M.B.2
  • 20
    • 0001003021 scopus 로고
    • Effect of osmoregulatory solutes on the stability of proteins
    • Gopal, S., and J. C. Ahluwalia. 1993. Effect of osmoregulatory solutes on the stability of proteins. J. Chem. Soc. Faraday Trans. 89:2769-2774.
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2769-2774
    • Gopal, S.1    Ahluwalia, J.C.2
  • 21
    • 0014930842 scopus 로고
    • Substrate-inhibited lactate dehydrogenase. Reaction mechanism and essential role of dissociated subunits
    • Griffin, J. H., and R. S. Criddle. 1970. Substrate-inhibited lactate dehydrogenase. Reaction mechanism and essential role of dissociated subunits. Biochemistry. 9:1195-1205.
    • (1970) Biochemistry , vol.9 , pp. 1195-1205
    • Griffin, J.H.1    Criddle, R.S.2
  • 22
    • 0015243640 scopus 로고
    • Cyanate formation in solutions of urea. I. Calculations of cyanate concentrations at different temperature and pH
    • Hagel, P., J. J. T. Gerding, W. Fieggen, and H. Bloemendal. 1971. Cyanate formation in solutions of urea. I. Calculations of cyanate concentrations at different temperature and pH. Biochim. Biophys. Acta. 243:366-373.
    • (1971) Biochim. Biophys. Acta. , vol.243 , pp. 366-373
    • Hagel, P.1    Gerding, J.J.T.2    Fieggen, W.3    Bloemendal, H.4
  • 24
    • 0015608870 scopus 로고
    • Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase
    • Holbrook, J. J., and V. A. Ingram. 1973. Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase. Biochem. J. 131: 729-738.
    • (1973) Biochem. J. , vol.131 , pp. 729-738
    • Holbrook, J.J.1    Ingram, V.A.2
  • 25
    • 77957095245 scopus 로고
    • Nonlinear least-squares analysis
    • Academic Press, San Diego
    • Johnson, M. L., and S. G. Frasier. 1985. Nonlinear least-squares analysis. In Enzyme Structure, Part J. Academic Press, San Diego. 301-342.
    • (1985) Enzyme Structure , Issue.PART J , pp. 301-342
    • Johnson, M.L.1    Frasier, S.G.2
  • 26
    • 0038624867 scopus 로고
    • Transfer free energies of some ions from water to dimethylsulfoxide-water and urea-water mixtures
    • Kundu, K. K., and A. K. Das. 1979. Transfer free energies of some ions from water to dimethylsulfoxide-water and urea-water mixtures. J. Solution Chem. 8:259-265.
    • (1979) J. Solution Chem. , vol.8 , pp. 259-265
    • Kundu, K.K.1    Das, A.K.2
  • 27
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee, J. C., and S. N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256:7193-7201.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 28
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolyte: Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
    • Lin, T.-Y., and S. N. Timasheff. 1994. Why do some organisms use a urea-methylamine mixture as osmolyte: thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. Biochemistry. 33:12695-12701.
    • (1994) Biochemistry , vol.33 , pp. 12695-12701
    • Lin, T.-Y.1    Timasheff, S.N.2
  • 29
    • 0028402540 scopus 로고
    • The effect of urea on the acitivity of lactate dehydrogenase from pig and skate muscles
    • in Russian
    • Lushchak, V. I., and L. P. Lushchak. 1994. The effect of urea on the acitivity of lactate dehydrogenase from pig and skate muscles. J. Evol. Biochem. Physiol. 30:185-191 (in Russian).
    • (1994) J. Evol. Biochem. Physiol. , vol.30 , pp. 185-191
    • Lushchak, V.I.1    Lushchak, L.P.2
  • 30
    • 0023444286 scopus 로고
    • Effects of urea and trimethylamine-N-oxide on enzyme activity and stability
    • Mashino, T., and I. Fridovich. 1987. Effects of urea and trimethylamine-N-oxide on enzyme activity and stability. Arch. Biochem. Biophys. 258:356-360.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 356-360
    • Mashino, T.1    Fridovich, I.2
  • 31
    • 0016169292 scopus 로고
    • Inhibition and activation of human lactate dehydrogenase by urea
    • McQueen, J. J. 1974. Inhibition and activation of human lactate dehydrogenase by urea. Ann. Clin. Biochem. 2:75-80.
    • (1974) Ann. Clin. Biochem. , vol.2 , pp. 75-80
    • McQueen, J.J.1
  • 32
    • 0027483576 scopus 로고
    • Determinants of relative amounts of medullary organic osmolytes: Effects of NaCl and urea differ
    • Nakanishi, T., O. Uyama, H. Nakahama, Y. Takamitsu, and M. Sugita. 1993. Determinants of relative amounts of medullary organic osmolytes: effects of NaCl and urea differ. Am. J. Physiol. 264:F472-F479.
    • (1993) Am. J. Physiol. , vol.264
    • Nakanishi, T.1    Uyama, O.2    Nakahama, H.3    Takamitsu, Y.4    Sugita, M.5
  • 33
    • 78651119214 scopus 로고
    • The solubility of amino acids and related compounds in aqueous urea solutions
    • Nozaki, Y., and C. Tanford. 1963. The solubility of amino acids and related compounds in aqueous urea solutions. J. Biol. Chem. 238:4074-4080.
    • (1963) J. Biol. Chem. , vol.238 , pp. 4074-4080
    • Nozaki, Y.1    Tanford, C.2
  • 34
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Academic Press, San Diego
    • Pace, C. N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. In Enzyme Structure, Part L. Academic Press, San Diego. 266-280.
    • (1986) Enzyme Structure , Issue.50 PART , pp. 266-280
    • Pace, C.N.1
  • 35
    • 0042404530 scopus 로고
    • Enzyme activities in concentrated solutions of glycinebetaine and other solutes
    • Pollard, A., and R. G. Wyn Jones. 1979. Enzyme activities in concentrated solutions of glycinebetaine and other solutes. Planta. 144:291-298.
    • (1979) Planta. , vol.144 , pp. 291-298
    • Pollard, A.1    Wyn Jones, R.G.2
  • 36
    • 0000433426 scopus 로고
    • Competitive inhibition of enzyme activity by urea
    • Rajagopalan, K. V., I. Fridovich, and P. Handler. 1961. Competitive inhibition of enzyme activity by urea. J. Biol. Chem. 236:1059-1065.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1059-1065
    • Rajagopalan, K.V.1    Fridovich, I.2    Handler, P.3
  • 37
    • 0026631716 scopus 로고
    • Increased thermal stability of proteins in the presence of naturally occurring osmolytes
    • Santoro, M. M., Y. Liu, S. M. A. Khan, L.-X. Hou, and D. W. Bolen. 1992. Increased thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry. 31:5278-5283.
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1    Liu, Y.2    Khan, S.M.A.3    Hou, L.-X.4    Bolen, D.W.5
  • 38
    • 0001837325 scopus 로고
    • From dogfish to dogs: Trimethylamines protect proteins from urea
    • Somero, G. N. 1986. From dogfish to dogs: trimethylamines protect proteins from urea. News Physiol. Sci. 1:9-12.
    • (1986) News Physiol. Sci. , vol.1 , pp. 9-12
    • Somero, G.N.1
  • 39
    • 0014010441 scopus 로고
    • Substrate and product inhibition of rabbit muscle lactic dehydrogenase heart and muscle isozymes
    • Stambaugh, R., and D. Post. 1966. Substrate and product inhibition of rabbit muscle lactic dehydrogenase heart and muscle isozymes. J. Biol. Chem. 241:1462-1467.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1462-1467
    • Stambaugh, R.1    Post, D.2
  • 40
    • 34250421107 scopus 로고
    • The role of proline accumulation in halophytes
    • Stewart, G. R., and J. A. Lee. 1974. The role of proline accumulation in halophytes. Planta. 120:279-289.
    • (1974) Planta. , vol.120 , pp. 279-289
    • Stewart, G.R.1    Lee, J.A.2
  • 42
    • 0029812281 scopus 로고    scopus 로고
    • Effect of proline on lactate dehydrogenase activity: Testing the generality and scope of the compatibility paradigm
    • Wang, A., and D. W. Bolen. 1996. Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm. Biophys. J. 71:2117-2122.
    • (1996) Biophys. J. , vol.71 , pp. 2117-2122
    • Wang, A.1    Bolen, D.W.2
  • 43
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang, A., and D. W. Bolen. 1997. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry. 36:9101-9108.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 44
    • 0344700633 scopus 로고
    • Multiple molecular forms of malic and lactic dehydrogenase during development
    • Wiggert, B., and C. Villee. 1964. Multiple molecular forms of malic and lactic dehydrogenase during development. J. Biol. Chem. 239:444-451.
    • (1964) J. Biol. Chem. , vol.239 , pp. 444-451
    • Wiggert, B.1    Villee, C.2
  • 45
    • 0017577228 scopus 로고
    • Interrelations between pH and temperature for the catlaytic rate of the M4 isozyme of lactate dehydrogenase (EC 1.1.1.27) from goldfish
    • Wilson, T. L. 1977. Interrelations between pH and temperature for the catlaytic rate of the M4 isozyme of lactate dehydrogenase (EC 1.1.1.27) from goldfish. Arch. Biochem. Biophys. 179:378-390.
    • (1977) Arch. Biochem. Biophys. , vol.179 , pp. 378-390
    • Wilson, T.L.1
  • 46
    • 0345562829 scopus 로고
    • Organ specificity and lactate-dehydrogenase activity: Differential inhibition by urea and related compounds
    • Withycombe, W. A., D. T. Plummer, and J. H. Wilkinson. 1965. Organ specificity and lactate-dehydrogenase activity: differential inhibition by urea and related compounds. Biochem. J. 94:384-389.
    • (1965) Biochem. J. , vol.94 , pp. 384-389
    • Withycombe, W.A.1    Plummer, D.T.2    Wilkinson, J.H.3
  • 47
    • 0001784001 scopus 로고
    • Organic osmotic effectors in cartilaginous fishes
    • Springer-Verlag, Berlin, Heidelberg
    • Yancey, P. H. 1985. Organic osmotic effectors in cartilaginous fishes. In Transport Processes, Iono-and Osmoregulation. Springer-Verlag, Berlin, Heidelberg. 424-436.
    • (1985) Transport Processes, Iono- and Osmoregulation , pp. 424-436
    • Yancey, P.H.1
  • 48
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P. H., M. E. Clark, S. C. Hand, R. D. Bowlus, and G. N. Somero. 1982. Living with water stress: evolution of osmolyte systems. Science. 217:1214-1222.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 49
    • 0001244253 scopus 로고
    • Urea-requiring lactate dehydrogenases of marine elasmobranch fishes
    • Yancey, P. H., and G. N. Somero. 1978. Urea-requiring lactate dehydrogenases of marine elasmobranch fishes. J. Comp. Physiol. 125:135-141.
    • (1978) J. Comp. Physiol. , vol.125 , pp. 135-141
    • Yancey, P.H.1    Somero, G.N.2
  • 50
    • 0018641198 scopus 로고
    • Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes
    • Yancey, P. H., and G. N. Somero. 1979. Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes. Biochem. J. 183:317-323.
    • (1979) Biochem. J. , vol.183 , pp. 317-323
    • Yancey, P.H.1    Somero, G.N.2
  • 51
    • 0001315798 scopus 로고
    • Methylamine osmoregulatory solutes of elasmogranch fishes counteract urea inhibition of enzymes
    • Yancey, P. H., and G. N. Somero. 1980. Methylamine osmoregulatory solutes of elasmogranch fishes counteract urea inhibition of enzymes. J. Exp. Zool. 212:205-213.
    • (1980) J. Exp. Zool. , vol.212 , pp. 205-213
    • Yancey, P.H.1    Somero, G.N.2
  • 52
    • 0000039143 scopus 로고
    • Kinetic studeies of rabbit muscle lactate dehydrogenase
    • Zewe, V., and H. J. Fromm. 1962. Kinetic studeies of rabbit muscle lactate dehydrogenase. J. Biol. Chem. 237:1668-1674.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1668-1674
    • Zewe, V.1    Fromm, H.J.2
  • 53
    • 0007285384 scopus 로고
    • Kinetic studies of rabbit muscle lactate dehydrogenase
    • Zewe, V., and H. J. Fromm. 1965. Kinetic studies of rabbit muscle lactate dehydrogenase. Biochemistry. 4:782-792.
    • (1965) Biochemistry , vol.4 , pp. 782-792
    • Zewe, V.1    Fromm, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.