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Volumn 8, Issue 1, 1996, Pages 41-47

High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ESCHERICHIA COLI;

EID: 0030219743     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0072     Document Type: Article
Times cited : (8)

References (21)
  • 1
    • 0015919107 scopus 로고
    • 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment
    • 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment. J. Biol. Chem. 248, 793-799.
    • (1973) J. Biol. Chem. , vol.248 , pp. 793-799
    • Spatz, L.1    Strittmatter, P.2
  • 3
  • 4
    • 0019298353 scopus 로고
    • 5-dependent microsomal fatty acid elongation and identification of products
    • 5-dependent microsomal fatty acid elongation and identification of products. J. Biol. Chem. 255, 11357-11364.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11357-11364
    • Keyes, S.R.1    Cinti, D.L.2
  • 5
    • 0017391211 scopus 로고
    • Mechanism of C-5 double bond introduction in the biosynthesis of cholesterol by rat liver microsomes
    • 5. Reddy, V. V. R., Kupfer, D., and Capsi, E. (1977) Mechanism of C-5 double bond introduction in the biosynthesis of cholesterol by rat liver microsomes. J. Biol. Chem. 252, 2797-2801.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2797-2801
    • Reddy, V.V.R.1    Kupfer, D.2    Capsi, E.3
  • 8
    • 0021645769 scopus 로고
    • 5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain
    • 5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain. J. Biol. Chem. 259, 13349-13354.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13349-13354
    • Ozols, J.1    Carr, S.A.2    Strittmatter, P.3
  • 10
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 16. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0024826342 scopus 로고
    • Conserved domains in molybdenum hydroxylases: The amino acid sequence of chicken hepatic sulfite oxidase
    • 17. Neame, P. J., and Barber, M. J. (1989) Conserved domains in molybdenum hydroxylases: The amino acid sequence of chicken hepatic sulfite oxidase. J. Biol. Chem. 264, 20894-20901.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20894-20901
    • Neame, P.J.1    Barber, M.J.2
  • 18
    • 0023057063 scopus 로고
    • Assimilatory nitrate reductase from Chlorella: Effect of ionic strength and pH on catalytic activity
    • 18. Kay, C. J., and Barber, M. J. (1986) Assimilatory nitrate reductase from Chlorella: Effect of ionic strength and pH on catalytic activity. J. Biol. Chem. 261, 14125-14129.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14125-14129
    • Kay, C.J.1    Barber, M.J.2
  • 19
    • 0030062088 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:Nitrate reductase
    • 19. Quinn, G. B., Trimboli, A. J., Prosser, I. M., and Barber, M. J. (1996) Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:nitrate reductase. Arch. Biochem. Biophys. 327, 151-160.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 151-160
    • Quinn, G.B.1    Trimboli, A.J.2    Prosser, I.M.3    Barber, M.J.4
  • 20
  • 21
    • 0021153567 scopus 로고
    • Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli
    • 21. Nagai, K., and Thogerson, H. C. (1984) Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nature 309, 810-812.
    • (1984) Nature , vol.309 , pp. 810-812
    • Nagai, K.1    Thogerson, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.