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Volumn 200, Issue 13, 1997, Pages 1839-1850

Amino acid sequence differences cannot fully explain interspecific variation in thermal sensitivities of Gobiid fish A4-lactate dehydrogenases (A4-LDHS)

Author keywords

Adaptation; Coryphopterus personatus; Coryphoterus nicholsi; Gillichthys mirabilis; Gillichthys seta; Gorby; Lactate dehydrogenase; Temperature

Indexed keywords


EID: 0030857260     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (48)

References (57)
  • 2
    • 0001236455 scopus 로고
    • Gobies of the genus Gillichthys with comments on the sensory canals as a taxonomic tool
    • BARLOW, G. W. (1961). Gobies of the genus Gillichthys with comments on the sensory canals as a taxonomic tool. Copeia 1961, 423-437.
    • (1961) Copeia , vol.1961 , pp. 423-437
    • Barlow, G.W.1
  • 3
    • 0022913133 scopus 로고
    • Estimating enzyme kinetic parameters: A computer program for linear regression and nonparametric analysis
    • BROOKS, S. P. J. AND SUELTER, C. H. (1986). Estimating enzyme kinetic parameters: A computer program for linear regression and nonparametric analysis. Int. J. Bio-med. Comput. 19, 89-99.
    • (1986) Int. J. Bio-med. Comput. , vol.19 , pp. 89-99
    • Brooks, S.P.J.1    Suelter, C.H.2
  • 5
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • CHOMCZYNSKI, P. AND SACCHI, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analyt. Biochem. 162, 156-159.
    • (1987) Analyt. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0027135040 scopus 로고
    • Kinetic and structural adaptations of cytoplasmic malate dehydrogenases of Eastern Pacific abalone (genus Haliotis) from different thermal habitats: Biochemical correlates of biogeographical patternins
    • DAHLHOFF, E. AND SOMERO, G. N. (1993). Kinetic and structural adaptations of cytoplasmic malate dehydrogenases of Eastern Pacific abalone (genus Haliotis) from different thermal habitats: biochemical correlates of biogeographical patternins. J. exp. Biol. 185, 137-150.
    • (1993) J. Exp. Biol. , vol.185 , pp. 137-150
    • Dahlhoff, E.1    Somero, G.N.2
  • 8
    • 0025651363 scopus 로고
    • Electrospray ionization mass spectrometry
    • ed. J. A. McCloskey, New York: Academic Press
    • EDMONDS, C. G. AND SMITH, R. D. (1990). Electrospray ionization mass spectrometry. In Methods in Enzymology, vol. 193, Mass Spectrometry (ed. J. A. McCloskey), pp. 412-431. New York: Academic Press.
    • (1990) Methods in Enzymology, Vol. 193, Mass Spectrometry , vol.193 , pp. 412-431
    • Edmonds, C.G.1    Smith, R.D.2
  • 9
    • 0025952257 scopus 로고
    • Oligodeoxyribonucleotide ligation to single-stranded cDNAs - A new tool for cloning 5′-ends of messenger RNAs and for constructing cDNA libraries by in vitro amplification
    • EDWARDS, J. B. D. M., DELORT, J. AND MALLET, J. (1991). Oligodeoxyribonucleotide ligation to single-stranded cDNAs - a new tool for cloning 5′-ends of messenger RNAs and for constructing cDNA libraries by in vitro amplification. Nucleic Acids Res. 19, 5227-5232.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5227-5232
    • Edwards, J.B.D.M.1    Delort, J.2    Mallet, J.3
  • 11
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNA's from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • FROHMAN, M. A., DUSH, M. K. AND MARTIN, G. R. (1988). Rapid production of full-length cDNA's from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc. natn. Acad. Sci. U.S.A. 85, 8998-9002.
    • (1988) Proc. Natn. Acad. Sci. U.S.A. , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 13
    • 0002721066 scopus 로고
    • The uses of heterochrony
    • ed. M. L. McKinney, New York: Plenum Press
    • GOULD, S. J. (1988). The uses of heterochrony. In Heterochrony in Evolution (ed. M. L. McKinney), pp. 1-13. New York: Plenum Press.
    • (1988) Heterochrony in Evolution , pp. 1-13
    • Gould, S.J.1
  • 14
    • 0002771750 scopus 로고
    • Electrophoretic and functional enzymic evolution in four species of eastern Pacific barracudas from different thermal environments
    • GRAVES, J. E. AND SOMERO, G. N. (1982). Electrophoretic and functional enzymic evolution in four species of eastern Pacific barracudas from different thermal environments. Evolution 36, 97-106.
    • (1982) Evolution , vol.36 , pp. 97-106
    • Graves, J.E.1    Somero, G.N.2
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • HARTL, F. U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 17
    • 0030896384 scopus 로고    scopus 로고
    • Evolution of lactate dehydrogenase-A homologs of barracuda fishes (Genus Sphyraena) from different thermal environments: Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site
    • HOLLAND, L. Z., MCFALL-NGAI, M. AND SOMERO, G. (1997). Evolution of lactate dehydrogenase-A homologs of barracuda fishes (Genus Sphyraena) from different thermal environments: Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site. Biochemistry 36, 3207-3215.
    • (1997) Biochemistry , vol.36 , pp. 3207-3215
    • Holland, L.Z.1    Mcfall-Ngai, M.2    Somero, G.3
  • 18
    • 0025604936 scopus 로고
    • Magnetic DNA hybridization properties of oligonucleotide probes attached to superparamagnetic beads and their use in the isolation of poly(A) mRNA from eukaryotic cells
    • HORNES, E. AND KORSNES, L. (1990). Magnetic DNA hybridization properties of oligonucleotide probes attached to superparamagnetic beads and their use in the isolation of poly(A) mRNA from eukaryotic cells. Genet. analyt. Tech. Appl. 7, 145-150.
    • (1990) Genet. Analyt. Tech. Appl. , vol.7 , pp. 145-150
    • Hornes, E.1    Korsnes, L.2
  • 19
    • 0000185790 scopus 로고
    • Changes in the fish fauna of Western North America correlated with changes in ocean temperature
    • HUBBS, C. L. (1948). Changes in the fish fauna of Western North America correlated with changes in ocean temperature. J. mar. Res. 7, 459-482.
    • (1948) J. Mar. Res. , vol.7 , pp. 459-482
    • Hubbs, C.L.1
  • 20
    • 0023038088 scopus 로고
    • A new way of enhancing the thermostability of proteases
    • IMANAKA, T., SHIBAZAKI, M. AND TAKAGI, M. (1986). A new way of enhancing the thermostability of proteases. Nature 324, 695-697.
    • (1986) Nature , vol.324 , pp. 695-697
    • Imanaka, T.1    Shibazaki, M.2    Takagi, M.3
  • 21
    • 0014939137 scopus 로고
    • Isoenzymes of Drosophila alcohol dehydrogenase
    • JACOBSON, K. B., MURPHY, J. B. AND HARTMAN, F. C. (1970). Isoenzymes of Drosophila alcohol dehydrogenase. J. biol. Chem. 245, 1075-1083.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1075-1083
    • Jacobson, K.B.1    Murphy, J.B.2    Hartman, F.C.3
  • 22
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • JAENICKE, R. (1991). Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 23
    • 0012129235 scopus 로고
    • Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases
    • JOHNSTON, I. A. AND WALESBY, N. J. (1977). Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases. J. comp. Physiol. 119, 195-206.
    • (1977) J. Comp. Physiol. , vol.119 , pp. 195-206
    • Johnston, I.A.1    Walesby, N.J.2
  • 24
    • 0023051846 scopus 로고
    • Conformational drift of dissociated lactate dehydrogenases
    • KING, L. AND WEBER, G. (1986a). Conformational drift of dissociated lactate dehydrogenases. Biochemistry 25, 3632-3637.
    • (1986) Biochemistry , vol.25 , pp. 3632-3637
    • King, L.1    Weber, G.2
  • 25
    • 0023051822 scopus 로고
    • Conformational drift and cryoinactivation of lactate dehydrogenase
    • KING, L. AND WEBER, G. (1986b). Conformational drift and cryoinactivation of lactate dehydrogenase. Biochemistry 25, 3637-3640.
    • (1986) Biochemistry , vol.25 , pp. 3637-3640
    • King, L.1    Weber, G.2
  • 26
    • 0027337514 scopus 로고
    • Divergence in proteins, mitochondrial DNA and reproductive compatibility across the isthmus of Panama
    • KNOWLTON, N., WEIGT, L. A., SOLORZANO, L. A., MILLS, D. K. AND BERMINGHAM, E. (1993). Divergence in proteins, mitochondrial DNA and reproductive compatibility across the isthmus of Panama. Science 260, 1629-1632.
    • (1993) Science , vol.260 , pp. 1629-1632
    • Knowlton, N.1    Weigt, L.A.2    Solorzano, L.A.3    Mills, D.K.4    Bermingham, E.5
  • 27
    • 0015146997 scopus 로고
    • Physical and chemical properties of reversibly inactivated lactate dehydrogenases
    • LEVI, A. S. AND KAPLAN, N. O. (1971). Physical and chemical properties of reversibly inactivated lactate dehydrogenases. J. biol. Chem. 246, 6409-6417.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6409-6417
    • Levi, A.S.1    Kaplan, N.O.2
  • 28
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • LINDQUIST, S. AND KIM, G. (1996). Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. natn. Acad. Sci. U.S.A. 93, 5301-5306.
    • (1996) Proc. Natn. Acad. Sci. U.S.A. , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 29
    • 0015990307 scopus 로고
    • Multiple forms of flounder muscle glyceraldehyde-3-phosphate dehydrogenase
    • MARANGOS, P. J. AND CONSTANTINIDES, S. M. (1974). Multiple forms of flounder muscle glyceraldehyde-3-phosphate dehydrogenase. J. biol. Chem. 249, 951-958.
    • (1974) J. Biol. Chem. , vol.249 , pp. 951-958
    • Marangos, P.J.1    Constantinides, S.M.2
  • 30
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • MATTHEWS, B. W., NICHOLSON, H. AND BECKTEL, W. J. (1987). Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. natn. Acad. Sci. U.S.A. 84, 6663-6667.
    • (1987) Proc. Natn. Acad. Sci. U.S.A. , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 31
    • 0025369515 scopus 로고
    • A comparative study of the thermal stability of the vertebrate eye lens: Antarctic fish to the desert iguana
    • MCFALL-NGAI, M. AND HORWITZ, J. (1990). A comparative study of the thermal stability of the vertebrate eye lens: Antarctic fish to the desert iguana. Exp. Eye Res. 50, 703-709.
    • (1990) Exp. Eye Res. , vol.50 , pp. 703-709
    • Mcfall-Ngai, M.1    Horwitz, J.2
  • 32
    • 0001300983 scopus 로고
    • Guide to the coastal marine fishes of California
    • MILLER, D. J. AND LEA, R. N. (1972). Guide to the coastal marine fishes of California. Cal. Fish Bull. 157.
    • (1972) Cal. Fish Bull. , vol.157
    • Miller, D.J.1    Lea, R.N.2
  • 33
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction
    • MULLIS, K. B. AND FALOONA, F. A. (1987). Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol. 155, 335-350.
    • (1987) Methods Enzymol. , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 34
    • 0015698372 scopus 로고
    • Biological functions of multistable proteins
    • NICKERSON, K. W. (1973). Biological functions of multistable proteins. J. theor. Biol. 40, 507-515.
    • (1973) J. Theor. Biol. , vol.40 , pp. 507-515
    • Nickerson, K.W.1
  • 35
    • 0027983128 scopus 로고
    • Acclimation temperature affects the functional and structural properties of lactate dehydrogenase from fish (Misgurnus fossilis) skeletal muscles
    • OZERNYUK, O. D., KLYACHKO, O. S. AND POLOSUKHINA, E. S. (1994). Acclimation temperature affects the functional and structural properties of lactate dehydrogenase from fish (Misgurnus fossilis) skeletal muscles. Comp. Biochem. Physiol. 107B, 141-145.
    • (1994) Comp. Biochem. Physiol. , vol.107 B , pp. 141-145
    • Ozernyuk, O.D.1    Klyachko, O.S.2    Polosukhina, E.S.3
  • 37
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • PATINO, M. M., LIU, J.-J., GLOVER, J. R. AND LINDQUIST, S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.-J.2    Glover, J.R.3    Lindquist, S.4
  • 38
    • 0021770240 scopus 로고
    • 4) allozymes of Fundulus heteroclitus
    • 4) allozymes of Fundulus heteroclitus. J. biol. Chem. 259, 1309-1318.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1309-1318
    • Place, A.R.1    Powers, D.A.2
  • 39
    • 0001979038 scopus 로고
    • A multidisciplinary approach to the selectionist/neutralist controversy using the model teleost, Fundulus heteroclitus
    • (ed. D. Futuyama and J. Antonovics), Oxford: Oxford University Press
    • POWERS, D. A., SMITH, M., GONZALEZ-VILLASENOR, I., DIMICHELLE, L., CRAWFORD, D., BERNARDI, G. AND LAUERMAN, T. (1993). A multidisciplinary approach to the selectionist/neutralist controversy using the model teleost, Fundulus heteroclitus. In Oxford Surveys in Evolutionary Biology, vol. 9 (ed. D. Futuyama and J. Antonovics), pp. 43-107. Oxford: Oxford University Press.
    • (1993) Oxford Surveys in Evolutionary Biology , vol.9 , pp. 43-107
    • Powers, D.A.1    Smith, M.2    Gonzalez-Villasenor, I.3    Dimichelle, L.4    Crawford, D.5    Bernardi, G.6    Lauerman, T.7
  • 40
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • PRUSINER, S. B. (1991). Molecular biology of prion diseases. Science 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 41
    • 0028132226 scopus 로고
    • Biology and genetics of prion diseases
    • PRUSINER, S. B. (1994). Biology and genetics of prion diseases. A. Rev. Microbiol. 48, 655-686.
    • (1994) A. Rev. Microbiol. , vol.48 , pp. 655-686
    • Prusiner, S.B.1
  • 42
    • 0023610359 scopus 로고
    • The synthesis and use of fluorescent oligonucleotides in DNA sequence analysis
    • SMITH, L. M., KAISER, R. J., SANDERS, J. Z. AND HOOD, L. E. (1987a). The synthesis and use of fluorescent oligonucleotides in DNA sequence analysis. Methods Enzymol. 155, 260-301.
    • (1987) Methods Enzymol. , vol.155 , pp. 260-301
    • Smith, L.M.1    Kaiser, R.J.2    Sanders, J.Z.3    Hood, L.E.4
  • 44
    • 0014575489 scopus 로고
    • Pyruvate kinase variants of the Alaskan kingcrab
    • SOMERO, G. N. (1969). Pyruvate kinase variants of the Alaskan kingcrab. Biochem. J. 114, 237-241.
    • (1969) Biochem. J. , vol.114 , pp. 237-241
    • Somero, G.N.1
  • 45
    • 0000132925 scopus 로고
    • pH-temperature interactions on proteins: Principles of optimal pH and buffer system design
    • SOMERO, G. N. (1981). pH-temperature interactions on proteins: principles of optimal pH and buffer system design. Mar. Biol. Lett. 2, 163-178.
    • (1981) Mar. Biol. Lett. , vol.2 , pp. 163-178
    • Somero, G.N.1
  • 46
    • 0028949615 scopus 로고
    • Proteins and temperature
    • SOMERO, G. N. (1995). Proteins and temperature. A. Rev. Physiol. 57, 43-68.
    • (1995) A. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 47
    • 0014410410 scopus 로고
    • Some distinctive properties of pyruvate kinase purified from rat liver
    • SUSOR, W. A. AND RUTTER, W. J. (1968). Some distinctive properties of pyruvate kinase purified from rat liver. Biochem. biophys. Res. Commun. 30, 14-20.
    • (1968) Biochem. Biophys. Res. Commun. , vol.30 , pp. 14-20
    • Susor, W.A.1    Rutter, W.J.2
  • 50
    • 0022999793 scopus 로고
    • Ligation of single-stranded oligodeoxyribonucleotides by T4 RNA ligase
    • TESSIER, D. C., BROUSSEAU, R. AND VERNET, T. (1986). Ligation of single-stranded oligodeoxyribonucleotides by T4 RNA ligase. Analyt. Biochem. 158, 171-178.
    • (1986) Analyt. Biochem. , vol.158 , pp. 171-178
    • Tessier, D.C.1    Brousseau, R.2    Vernet, T.3
  • 52
    • 0020458617 scopus 로고
    • 10 values of the laclate dehydrogenase reaction
    • 10 values of the laclate dehydrogenase reaction. Can. J. Zool. 60, 1293-1299.
    • (1982) Can. J. Zool. , vol.60 , pp. 1293-1299
    • Walsh, P.J.1    Somero, G.N.2
  • 53
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • WILKINSON, G. N. (1961). Statistical estimations in enzyme kinetics. Biochem. J. 80, 323-332.
    • (1961) Biochem. J. , vol.80 , pp. 323-332
    • Wilkinson, G.N.1
  • 54
    • 0028934277 scopus 로고
    • Differences in the chemical reactivity of individual molecules of an enzyme
    • XUE, Q. AND YEUNG, E. S. (1995). Differences in the chemical reactivity of individual molecules of an enzyme. Nature 373, 681-683.
    • (1995) Nature , vol.373 , pp. 681-683
    • Xue, Q.1    Yeung, E.S.2
  • 56
    • 0000646969 scopus 로고
    • m values of vertebrate lactate dehydrogenases
    • m values of vertebrate lactate dehydrogenases. J. comp. Physiol. 125B, 129-134.
    • (1978) J. Comp. Physiol. , vol.125 B , pp. 129-134
    • Yancey, P.H.1    Somero, G.N.2


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