메뉴 건너뛰기




Volumn 323, Issue 2, 2004, Pages 505-511

Purification and characterization of mouse CYP27B1 overproduced by an Escherichia coli system coexpressing molecular chaperonins GroEL/ES

Author keywords

CYP27B1; GroEL ES; Molecular chaperonin; Vitamin D 1 hydroxylation; Vitamin D 25 hydroxylation

Indexed keywords

ALFACALCIDOL; CALCIFEDIOL; CHAPERONIN; COLECALCIFEROL; CYTOCHROME; CYTOCHROME P450; CYTOCHROME P450 105A1; CYTOCHROME P450 27B1; UNCLASSIFIED DRUG;

EID: 4544258603     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.110     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 0028988403 scopus 로고
    • Structureâ€"function relationships in vitamin D endocrine system
    • R. Boullion, W.H. Okamura, and A.W. Norman Structureâ€" function relationships in vitamin D endocrine system Endocr. Rev. 16 1995 200 257
    • (1995) Endocr. Rev. , vol.16 , pp. 200-257
    • Boullion, R.1    Okamura, W.H.2    Norman, A.W.3
  • 3
    • 0015240863 scopus 로고
    • Identification of 1,25-dihydroxycholestecalciferol, a new kidney hormone controlling calcium metabolism
    • D.E.M. Lawson, D.R. Fraser, E. Kodicek, H.R. Morris, and D.H. Williams Identification of 1,25-dihydroxycholestecalciferol, a new kidney hormone controlling calcium metabolism Nature 230 1971 228 230
    • (1971) Nature , vol.230 , pp. 228-230
    • Lawson, D.E.M.1    Fraser, D.R.2    Kodicek, E.3    Morris, H.R.4    Williams, D.H.5
  • 5
    • 0015113986 scopus 로고
    • Regulation by calcium of in vivo synthesis of 1,25- dihydroxycholestecalciferol and 21,25-dihydroxycholestecalciferol
    • I.T. Boyle, R.W. Gray, and H.F. DeLuca Regulation by calcium of in vivo synthesis of 1,25-dihydroxycholestecalciferol and 21,25- dihydroxycholestecalciferol Proc. Natl. Acad. Sci. USA 68 1971 2131 2134
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2131-2134
    • Boyle, I.T.1    Gray, R.W.2    Deluca, H.F.3
  • 13
  • 14
    • 0031593494 scopus 로고    scopus 로고
    • Two novel 1α-hydroxylase mutations in French-Canadians with vitamin D dependency rickets type I
    • T. Yoshida, T. Monkawa, H.S. Tenenhouse, P. Goodyer, T. Shinki, T. Suda, and S. Wakino Two novel 1α-hydroxylase mutations in French-Canadians with vitamin D dependency rickets type I Kidney Int. 54 1998 1437 1443
    • (1998) Kidney Int. , vol.54 , pp. 1437-1443
    • Yoshida, T.1    Monkawa, T.2    Tenenhouse, H.S.3    Goodyer, P.4    Shinki, T.5    Suda, T.6    Wakino, S.7
  • 16
    • 0035663972 scopus 로고    scopus 로고
    • Structureâ€"function analysis of CYP27B1 and CYP27A1, Studied on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX)
    • N. Sawada, T. Sakaki, S. Kitanaka, S. Kato, and K. Inouye Structureâ€"function analysis of CYP27B1 and CYP27A1, Studied on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX) Eur. J. Biochem. 268 2001 6607 6615
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6607-6615
    • Sawada, N.1    Sakaki, T.2    Kitanaka, S.3    Kato, S.4    Inouye, K.5
  • 17
    • 0035883794 scopus 로고    scopus 로고
    • Osmotic stress induced by carbohydrate enhances expression of foreign proteins in Escherichia coli
    • N. Kagawa, and Q. Cao Osmotic stress induced by carbohydrate enhances expression of foreign proteins in Escherichia coli Arch. Biochem. Biophys. 393 2001 290 296
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 290-296
    • Kagawa, N.1    Cao, Q.2
  • 19
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaKâ€"DnaJâ€"GrpE and GroELâ€" GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • K. Nishihara, M. Kanemori, M. Kitagawa, H. Yanagi, and T. Yura Chaperone coexpression plasmids: differential and synergistic roles of DnaKâ€"DnaJâ€"GrpE and GroELâ€" GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli Appl. Environ. Microbiol. 64 1998 1694 1699
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 20
    • 0033551262 scopus 로고    scopus 로고
    • Electrostatic interaction between cytochrome P450 and NADPH-P450 reductase: Comparison of mixed and fused systems consisting of rat cytochrome P450 1A1 and yeast NADPH-P450 reductase
    • S. Kondo, T. Sakaki, H. Ohkawa, and K. Inouye Electrostatic interaction between cytochrome P450 and NADPH-P450 reductase: comparison of mixed and fused systems consisting of rat cytochrome P450 1A1 and yeast NADPH-P450 reductase Biochem. Biophys. Res. Commun. 257 1999 273 278
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 273-278
    • Kondo, S.1    Sakaki, T.2    Ohkawa, H.3    Inouye, K.4
  • 21
    • 0000622703 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes J. Biol. Chem. 118 1964 397 404
    • (1964) J. Biol. Chem. , vol.118 , pp. 397-404
    • Omura, T.1    Sato, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.