메뉴 건너뛰기




Volumn 72, Issue 9, 2008, Pages 2448-2451

Yak lactate dehydgogenase A4: Purification, properties, and cDNA cloning

Author keywords

Lactate dehydrogenase A; Molecular adaptation; Purification; Yak

Indexed keywords

AMINES; AMINO ACIDS; CLONING; ORGANIC ACIDS; PURIFICATION;

EID: 52649128817     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80208     Document Type: Article
Times cited : (8)

References (16)
  • 1
    • 0031966661 scopus 로고    scopus 로고
    • The structural basis of molecular adaptation
    • Golding, G. B., and Dean, A. M., The structural basis of molecular adaptation. Mol. Biol. Evol., 15, 355-369 (1998).
    • (1998) Mol. Biol. Evol , vol.15 , pp. 355-369
    • Golding, G.B.1    Dean, A.M.2
  • 3
    • 0035988466 scopus 로고    scopus 로고
    • Polymorphism in mitochondrial DNA (mtDNA) of yak (Bos grunniens)
    • Tu, Z. C., Qiu, H., and Zhang, Y. P., Polymorphism in mitochondrial DNA (mtDNA) of yak (Bos grunniens). Biochem. Genet., 40, 187-193 (2002).
    • (2002) Biochem. Genet , vol.40 , pp. 187-193
    • Tu, Z.C.1    Qiu, H.2    Zhang, Y.P.3
  • 4
    • 0021099625 scopus 로고
    • Evolutionary relationships of vertebrate lactate dehydrogenase isozymes A4 (muscle), B4 (heart), and C4 (testis)
    • Li, S. S., Fitch, W. M., Pan, Y. C., and Sharief, F. S., Evolutionary relationships of vertebrate lactate dehydrogenase isozymes A4 (muscle), B4 (heart), and C4 (testis). J. Biol. Chem., 258, 7029-7032 (1983).
    • (1983) J. Biol. Chem , vol.258 , pp. 7029-7032
    • Li, S.S.1    Fitch, W.M.2    Pan, Y.C.3    Sharief, F.S.4
  • 5
    • 0024690076 scopus 로고
    • Lactate dehydrogenase-B cDNA from the teleost Fundulus heteroclitus: Evolutionary implications
    • Crawford, D. L., Constantino, H. R., and Powers, D. A., Lactate dehydrogenase-B cDNA from the teleost Fundulus heteroclitus: evolutionary implications. Mol. Biol. Evol., 6, 369-383 (1989).
    • (1989) Mol. Biol. Evol , vol.6 , pp. 369-383
    • Crawford, D.L.1    Constantino, H.R.2    Powers, D.A.3
  • 6
    • 0025003067 scopus 로고
    • Primary structure of bovine lactate dehydrogenase-A isozyme and its synthesis in Escherichia coli
    • Ishiguro, N., Osame, S., Kagiya, R., Ichijo, S., and Shinagawa, M., Primary structure of bovine lactate dehydrogenase-A isozyme and its synthesis in Escherichia coli. Gene, 91, 281-285 (1990).
    • (1990) Gene , vol.91 , pp. 281-285
    • Ishiguro, N.1    Osame, S.2    Kagiya, R.3    Ichijo, S.4    Shinagawa, M.5
  • 7
    • 0027959391 scopus 로고
    • The nucleotide and deduced amino-acid sequences of a cDNA encoding lactate dehydrogenase from Caenorhabditis elegans: The evolutionary relationships of lactate dehydrogenases from mammals, birds, amphibians, fish, nematodes, plants, bacteria, mycoplasma, and plasmodium
    • Tsoi, S. C., and Li, S. S., The nucleotide and deduced amino-acid sequences of a cDNA encoding lactate dehydrogenase from Caenorhabditis elegans: the evolutionary relationships of lactate dehydrogenases from mammals, birds, amphibians, fish, nematodes, plants, bacteria, mycoplasma, and plasmodium. Biochem. Biophys. Res. Commun., 205, 558-564 (1994).
    • (1994) Biochem. Biophys. Res. Commun , vol.205 , pp. 558-564
    • Tsoi, S.C.1    Li, S.S.2
  • 8
    • 0023645872 scopus 로고
    • The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surface
    • Wigley, D. B., Clarke, A. R., Dunn, C. R., Barstow, D. A., Atkinson, T., Chia, W. N., Muirhead, H., and Holbrook, J. J., The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surface. Biochim. Biophys. Acta, 916, 145-148 (1987).
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 145-148
    • Wigley, D.B.1    Clarke, A.R.2    Dunn, C.R.3    Barstow, D.A.4    Atkinson, T.5    Chia, W.N.6    Muirhead, H.7    Holbrook, J.J.8
  • 9
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution
    • Wigley, D. B., Gamblin, S. J., Turkenburg, J. P., Dodson, E. J., Piontek, K., Muirhead, H., and Holbrook, J. J., Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution. J. Mol. Biol., 223, 317-335 (1992).
    • (1992) J. Mol. Biol , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7
  • 10
    • 0025191073 scopus 로고
    • A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme
    • Feeney, R., Clarke, A. R., and Holbrook, J. J., A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme. Biochem. Biophys. Res. Commun., 166, 667-672 (1990).
    • (1990) Biochem. Biophys. Res. Commun , vol.166 , pp. 667-672
    • Feeney, R.1    Clarke, A.R.2    Holbrook, J.J.3
  • 11
    • 0028271650 scopus 로고
    • Source of catalysis in the lactate dehydrogenase system: Ground-state interactions in the enzyme-substrate complex
    • Deng, H., Zheng, J., Clarke, A., Holbrook, J. J., Callender, R., and Burgner, J. W., Source of catalysis in the lactate dehydrogenase system: ground-state interactions in the enzyme-substrate complex. Biochemistry, 33, 2297-2305 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2297-2305
    • Deng, H.1    Zheng, J.2    Clarke, A.3    Holbrook, J.J.4    Callender, R.5    Burgner, J.W.6
  • 12
    • 0028223910 scopus 로고
    • Substitution of the amino acid at position 102 with polar and aromatic residues influences substrate specificity of lactate dehydrogenase
    • Nicholls, D. J., Davey, M., Jones, S. E., Miller, J., Holbrook, J. J., Clarke, A. R., Scawen, M. D., Atkinson, T., and Goward, C. R., Substitution of the amino acid at position 102 with polar and aromatic residues influences substrate specificity of lactate dehydrogenase. J. Protein Chem., 13, 129-133 (1994).
    • (1994) J. Protein Chem , vol.13 , pp. 129-133
    • Nicholls, D.J.1    Davey, M.2    Jones, S.E.3    Miller, J.4    Holbrook, J.J.5    Clarke, A.R.6    Scawen, M.D.7    Atkinson, T.8    Goward, C.R.9
  • 13
    • 0032310891 scopus 로고    scopus 로고
    • Integrated removal of nucleic acids and recovery of LDH from homogenate of beef heart by affinity precipitation
    • Dissing, U., and Mattiasson, B., Integrated removal of nucleic acids and recovery of LDH from homogenate of beef heart by affinity precipitation. Bioseparation, 7, 221-229 (1998).
    • (1998) Bioseparation , vol.7 , pp. 221-229
    • Dissing, U.1    Mattiasson, B.2
  • 14
    • 0028998625 scopus 로고
    • Intracellular localization of the testicular and sperm-specific lactate dehydrogenase isozyme C4 in mice
    • Burgos, C., Maldonado, C., Gerez de Burgos, N. M., Aoki, A., and Blanco, A., Intracellular localization of the testicular and sperm-specific lactate dehydrogenase isozyme C4 in mice. Biol. Reprod., 53, 84-92 (1995).
    • (1995) Biol. Reprod , vol.53 , pp. 84-92
    • Burgos, C.1    Maldonado, C.2    Gerez de Burgos, N.M.3    Aoki, A.4    Blanco, A.5
  • 15
    • 0029815403 scopus 로고    scopus 로고
    • Purification and characterization of lactate dehydrogenase isoenzymes 1 and 2 from Molinema dessetae (Nematoda: Filarioidea)
    • Marchat, L., Loiseau, P. M., and Petek, F., Purification and characterization of lactate dehydrogenase isoenzymes 1 and 2 from Molinema dessetae (Nematoda: Filarioidea). Parasitol. Res., 82, 672-680 (1996).
    • (1996) Parasitol. Res , vol.82 , pp. 672-680
    • Marchat, L.1    Loiseau, P.M.2    Petek, F.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.