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Volumn 54, Issue 1, 2004, Pages 87-93

Production of D-glucose dehydrogenase for the determination of D-glucose

Author keywords

Bacillus thuringiensis M15; D glucose dehydrogenase; Production

Indexed keywords

BACILLUS THURINGIENSIS; VISCUM; VISCUM ALBUM;

EID: 1842843877     PISSN: 15904261     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (14)
  • 1
    • 1842867516 scopus 로고
    • D-glucose dehydrogenase from Gluconobacter suboxydans
    • Adachi O., Ameyama M. (1982). D-glucose dehydrogenase from Gluconobacter suboxydans. Method. Enzymol., 89: 159-163.
    • (1982) Method. Enzymol. , vol.89 , pp. 159-163
    • Adachi, O.1    Ameyama, M.2
  • 2
    • 0026021702 scopus 로고
    • Glucose dehydrogenase from Bacillus subtilis expressed in Escherichia coli I: Purification, characterization and comparison with glucose dehydrogenase from Bacillus megaterium
    • Hilt W., Pfleiderer G., Fortnagel P. (1991). Glucose dehydrogenase from Bacillus subtilis expressed in Escherichia coli I: purification, characterization and comparison with glucose dehydrogenase from Bacillus megaterium. Biochim. Biophys. Acta, 1076: 298-304.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 298-304
    • Hilt, W.1    Pfleiderer, G.2    Fortnagel, P.3
  • 3
    • 0024569098 scopus 로고
    • The influence of the culture pH value on the direct glucose oxidative pathway of Klebsiella pneumoniae NCTC 418
    • Hommes R.W., Postma P.W., Tempest D.W., Neijssel O.M. (1989). The influence of the culture pH value on the direct glucose oxidative pathway of Klebsiella pneumoniae NCTC 418. Arch. Microb., 151 (3): 261-267.
    • (1989) Arch. Microb. , vol.151 , Issue.3 , pp. 261-267
    • Hommes, R.W.1    Postma, P.W.2    Tempest, D.W.3    Neijssel, O.M.4
  • 4
    • 0027325779 scopus 로고
    • Microbiosensor for acetylcholine and glucose
    • Karube I., Yokoyama K., Tomiya E. (1993). Microbiosensor for acetylcholine and glucose. Biosens. Bioelec., 8(3-4): 219-228.
    • (1993) Biosens. Bioelec. , vol.8 , Issue.3-4 , pp. 219-228
    • Karube, I.1    Yokoyama, K.2    Tomiya, E.3
  • 6
    • 0020435678 scopus 로고
    • D-glucose dehydrogenase from Pseudomonas fluorescens, membrane bound
    • Matsushita K., Ameyama M. (1982). D-glucose dehydrogenase from Pseudomonas fluorescens, membrane bound. Method. Enzymol., 89: 149-154.
    • (1982) Method. Enzymol. , vol.89 , pp. 149-154
    • Matsushita, K.1    Ameyama, M.2
  • 7
    • 0024553766 scopus 로고
    • Relativity with ubiquinone of quinoprotein D-glucose dehydrogenase from Gluconobacter suboxydans
    • Matsushita K., Shinagawa E., Adachi O., Ameyama M. (1989). Relativity with ubiquinone of quinoprotein D-glucose dehydrogenase from Gluconobacter suboxydans. J. Biochem., 105: 633-637.
    • (1989) J. Biochem. , vol.105 , pp. 633-637
    • Matsushita, K.1    Shinagawa, E.2    Adachi, O.3    Ameyama, M.4
  • 8
    • 0020071306 scopus 로고
    • The role of oxygen in the regulation of glucose metabolism, transport and the tricarboxylic acid cycle in Pseudomonas aeruginosa
    • Michell G.G., Dawes E.A. (1982). The role of oxygen in the regulation of glucose metabolism, transport and the tricarboxylic acid cycle in Pseudomonas aeruginosa. J. Gen. Microbiol., 128: 49-59.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 49-59
    • Michell, G.G.1    Dawes, E.A.2
  • 9
    • 0024815755 scopus 로고
    • Enzymatic properties of isozyme and variants of glucose dehydrogenase from Bacillus megaterium
    • Mitamaru T., Urabe I., Okada H. (1989). Enzymatic properties of isozyme and variants of glucose dehydrogenase from Bacillus megaterium. Eur. J. Biochem., 186: 389-393.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 389-393
    • Mitamaru, T.1    Urabe, I.2    Okada, H.3
  • 10
    • 0015413828 scopus 로고
    • Gluconate regulation of glucose catabolism in Pseudomonas fluorescens
    • Quay S.C., Friedman S.B., Eisenberg R.C. (1972). Gluconate regulation of glucose catabolism in Pseudomonas fluorescens. J. Bacteriol., 112: 291-298.
    • (1972) J. Bacteriol. , vol.112 , pp. 291-298
    • Quay, S.C.1    Friedman, S.B.2    Eisenberg, R.C.3
  • 11
    • 0005956556 scopus 로고
    • Glucose dehydrogenase-soluble
    • Sadoff H.L. (1966). Glucose dehydrogenase-soluble. Method. Enzymol., 9: 103-107.
    • (1966) Method. Enzymol. , vol.9 , pp. 103-107
    • Sadoff, H.L.1
  • 12
    • 0024489201 scopus 로고
    • Effect of growth rate and oxygen tension on glucose dehydrogenase activity in Acinetobacter calcoaceticus LMD 79.41
    • Van Schie B.J., Van Dijken J.P., Kuenen J.G. (1988). Effect of growth rate and oxygen tension on glucose dehydrogenase activity in Acinetobacter calcoaceticus LMD 79.41. Antonie van Leeuwenhoek, 55: 53-65.
    • (1988) Antonie Van Leeuwenhoek , vol.55 , pp. 53-65
    • Van Schie, B.J.1    Van Dijken, J.P.2    Kuenen, J.G.3
  • 13
    • 1842845580 scopus 로고
    • Continuous culture studies on the regulation of PQQ-dependent glucose dehydrogenase in Acinetobacter calcoaceticus
    • Visser W., Schie van B.J., Bont de J.A.M., Dijken van J.P., Kuenen J.G. (1985). Continuous culture studies on the regulation of PQQ-dependent glucose dehydrogenase in Acinetobacter calcoaceticus. Antonie van Leeuwenhoek, 51: 563.
    • (1985) Antonie Van Leeuwenhoek , vol.51 , pp. 563
    • Visser, W.1    Van Schie, B.J.2    De Bont, J.A.M.3    Van Dijken, J.P.4    Kuenen, J.G.5
  • 14
    • 0027393952 scopus 로고
    • Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression
    • Yamada M., Asaoka S., Saier M.H. Jr., Yamada Y. (1993). Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression. J. Bacteriol., 175(2): 568-571.
    • (1993) J. Bacteriol. , vol.175 , Issue.2 , pp. 568-571
    • Yamada, M.1    Asaoka, S.2    Saier Jr., M.H.3    Yamada, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.