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Volumn 30, Issue 6, 1998, Pages 583-584

Overexpression, purification and characterization, of thermostable catechol 2,3-dioxygenase

Author keywords

Catechol 2,3 dioxygenase; Circular dichroism; Intrinsic fluorescence spectrum

Indexed keywords


EID: 0006033541     PISSN: 05829879     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (9)
  • 1
    • 0026723792 scopus 로고
    • Molecular cloning and mapping of phenol degradation genes from Bacillus stearothermophilus FDTP - 3 and their expression in Escherichia coli
    • Dong F M et al. Molecular cloning and mapping of phenol degradation genes from Bacillus stearothermophilus FDTP - 3 and their expression in Escherichia coli. Appl Environ Microbiol, 1992, 58: 2531-2535
    • (1992) Appl Environ Microbiol , vol.58 , pp. 2531-2535
    • Dong, F.M.1
  • 3
    • 0023254924 scopus 로고
    • Inducible expression vectors incorporating the Escherichia coli atpE, translational initiation region
    • Schauder B et al. Inducible expression vectors incorporating the Escherichia coli atpE, translational initiation region. Gene, 1987, 52: 279-283
    • (1987) Gene , vol.52 , pp. 279-283
    • Schauder, B.1
  • 4
    • 0028988356 scopus 로고
    • Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered E. coli
    • Kobayashi T et al. Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered E. coli. J Biochem, 1994, 117: 614-622
    • (1994) J Biochem , vol.117 , pp. 614-622
    • Kobayashi, T.1
  • 5
    • 0026067002 scopus 로고
    • Physicochemical characterization of bovine retinal arrestin
    • Susan K et al. Physicochemical characterization of bovine retinal arrestin. Arch Biochem Biophys, 1991, 285: 126-133
    • (1991) Arch Biochem Biophys , vol.285 , pp. 126-133
    • Susan, K.1
  • 6
    • 0026566944 scopus 로고
    • Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus, thermal denaturation and activation
    • Horst K et al. Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus, thermal denaturation and activation. J Biol Chem, 1992, 267: 22681-22685
    • (1992) J Biol Chem , vol.267 , pp. 22681-22685
    • Horst, K.1
  • 7
    • 0014429573 scopus 로고
    • Metapyrocatechase, the role of iron and sulfhydryl groups
    • Mitsuhiro Nozaki et al. Metapyrocatechase, the role of iron and sulfhydryl groups. J Biol Chem, 1968, 243: 2682-2690
    • (1968) J Biol Chem , vol.243 , pp. 2682-2690
    • Nozaki, M.1
  • 8
    • 14744273210 scopus 로고
    • A Pseudomonas putida strain able to degrade m-toluate in the presence of 3-chlorocatechol
    • Wasserfallen A et al. A Pseudomonas putida strain able to degrade m-toluate in the presence of 3-chlorocatechol. Bio/Technology, 1991, 9: 296-298
    • (1991) Bio/Technology , vol.9 , pp. 296-298
    • Wasserfallen, A.1
  • 9
    • 0028864185 scopus 로고
    • Irreversible thermal denaturation of Torpedo californica acetylcholinesterase
    • David I K et al. Irreversible thermal denaturation of Torpedo californica acetylcholinesterase. Protein Science, 1995, 4: 2349-2357
    • (1995) Protein Science , vol.4 , pp. 2349-2357
    • David, I.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.