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Volumn 15, Issue 3, 1999, Pages 344-348

Purification and stabilization of a monomeric isocitrate dehydrogenase from Corynebacterium glutamicum

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; FRACTIONATION; GEL CHROMATOGRAPHY; GEL FILTRATION; ION EXCHANGE CHROMATOGRAPHY; ISOCITRATE DEHYDROGENASE; PLASMID; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RECOMBINANT ENZYME;

EID: 0033117353     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1034     Document Type: Article
Times cited : (21)

References (10)
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    • (1995) Science , vol.268 , pp. 1312-1318
    • Bolduc, J.M.1    Dyer, D.H.2    Scott, W.G.3    Singer, P.4    Sweet, R.M.5    Koshland D.E., Jr.6    Stoddard, B.L.7
  • 2
    • 0000980429 scopus 로고
    • Stucture, function and regulation of NAD- And NADP-isocitrate dehydrogenases in higher plants and in other organisms
    • Chen R. D., Gadal P. Stucture, function and regulation of NAD- and NADP-isocitrate dehydrogenases in higher plants and in other organisms. Plant Physiol. Biochem. 28:1990;411-427.
    • (1990) Plant Physiol. Biochem. , vol.28 , pp. 411-427
    • Chen, R.D.1    Gadal, P.2
  • 3
    • 0026075229 scopus 로고
    • Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacteriumRhodomicrobium vanniellii.
    • Leyland M. L., Kelley R. Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacteriumRhodomicrobium vanniellii. Eur. J. Biochem. 202:1991;85-93.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 85-93
    • Leyland, M.L.1    Kelley, R.2
  • 4
    • 0027064487 scopus 로고
    • Purification and characterization of monomeric isocitrate dehydrogenase with NADP-specificity fromVibrio parahaemolyticus
    • Fukunaga N. S., Sahara I. T., Ishii S. A., Suzuki M. Purification and characterization of monomeric isocitrate dehydrogenase with NADP-specificity fromVibrio parahaemolyticus. J. Biochem. 112:1992;849-855.
    • (1992) J. Biochem. , vol.112 , pp. 849-855
    • Fukunaga, N.S.1    Sahara, I.T.2    Ishii, S.A.3    Suzuki, M.4
  • 5
    • 0027508357 scopus 로고
    • Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium,Vibrio
    • Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N. Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium,Vibrio. J. Bacteriol. 175:1993;6873-6880.
    • (1993) J. Bacteriol. , vol.175 , pp. 6873-6880
    • Ishii, A.1    Suzuki, M.2    Sahara, T.3    Takada, Y.4    Sasaki, S.5    Fukunaga, N.6
  • 6
    • 0028942304 scopus 로고
    • Cloning, sequence analysis, expression, and inactivation ofthe Corynebacterium glutamicum icd
    • Eikmanns B. J., Rittmann D., Sahm H. Cloning, sequence analysis, expression, and inactivation ofthe Corynebacterium glutamicum icd. J. Bacteriol. 177:1995;774-782.
    • (1995) J. Bacteriol. , vol.177 , pp. 774-782
    • Eikmanns, B.J.1    Rittmann, D.2    Sahm, H.3
  • 9
    • 0029557251 scopus 로고
    • A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity
    • Chen R. D., Greer A., Dean A. D. A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proc. Natl. Acad. Sci. USA. 92:1995;11666-11670.
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    • Chen, R.D.1    Greer, A.2    Dean, A.D.3
  • 10
    • 0024288496 scopus 로고
    • Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum
    • Chen R. D., Le Marrechal P., Vidal J., Jacquot J. P., Gadal P. Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum. Eur. J. Biochem. 175:1988;565-572.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.