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Volumn 30, Issue 4, 2008, Pages 625-630

Expression, purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, Bombyx mori, pupae expression system

Author keywords

Baculovirus; Glycosylation; Protein disulfide isomerase; Protein expression; Silkworm pupae

Indexed keywords

ENZYME INHIBITION; GENE EXPRESSION; GLYCOSYLATION; POLYPEPTIDES; PROTEINS; YEAST;

EID: 43149104775     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-007-9582-4     Document Type: Article
Times cited : (3)

References (22)
  • 1
    • 0025773714 scopus 로고
    • Asparagine-linked oligosaccharide processing in lepidopteran insect cells temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells
    • Davidson DJ, Castellino FJ (1991a) Asparagine-linked oligosaccharide processing in lepidopteran insect cells temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells. Biochemistry 30:6167-6174
    • (1991) Biochemistry , vol.30 , pp. 6167-6174
    • Davidson, D.J.1    Castellino, F.J.2
  • 2
    • 0025741695 scopus 로고
    • Structures of the asparagine-289-linked oligosaccharides assembled on recombinant human plasminogen expressed in a Mamestra brassicae cell line (IZD-MB0503)
    • Davidson DJ, Castellino FJ (1991b) Structures of the asparagine-289- linked oligosaccharides assembled on recombinant human plasminogen expressed in a Mamestra brassicae cell line (IZD-MB0503). Biochemistry 30:6689-6696
    • (1991) Biochemistry , vol.30 , pp. 6689-6696
    • Davidson, D.J.1    Castellino, F.J.2
  • 3
    • 0025336176 scopus 로고
    • Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson DJ, Fraser MJ, Castellino FJ (1990) Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry 29:5584-5590
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.1    Fraser, M.J.2    Castellino, F.J.3
  • 4
    • 0025996759 scopus 로고
    • [alpha]-Mannosidase-catalyzed trimming of high-mannose glycans in noninfected and baculovirus-infected Spodoptera frugiperda cells (IPLB-SF-21AE). a possible contributing regulatory mechanism for assembly of complex-type oligosaccharides in infected cells
    • Davidson DJ, Bretthauer RK, Castellino FJ (1991) [alpha]-Mannosidase- catalyzed trimming of high-mannose glycans in noninfected and baculovirus-infected Spodoptera frugiperda cells (IPLB-SF-21AE). A possible contributing regulatory mechanism for assembly of complex-type oligosaccharides in infected cells. Biochemistry 30:9811-9815
    • (1991) Biochemistry , vol.30 , pp. 9811-9815
    • Davidson, D.J.1    Bretthauer, R.K.2    Castellino, F.J.3
  • 5
    • 0028793359 scopus 로고
    • Intrinsic glycosylation potentials of insect cell cultures and insect larvae
    • Davis TR, Wood HA (1995) Intrinsic glycosylation potentials of insect cell cultures and insect larvae. In Vitro Cell Dev Biol 31:659-663
    • (1995) In Vitro Cell Dev Biol , vol.31 , pp. 659-663
    • Davis, T.R.1    Wood, H.A.2
  • 6
    • 43149117632 scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert HF (1990) Protein disulfide isomerase and assisted protein folding. J Biol Chem 272: 505-511
    • (1990) J Biol Chem , vol.272 , pp. 505-511
    • Gilbert, H.F.1
  • 7
    • 0029620311 scopus 로고
    • Protein disulfide isomerase mutant lacking isomerase activity accelerates protein folding in the cell
    • Hayano T, Hirose M, Kikuchi M (1995) Protein disulfide isomerase mutant lacking isomerase activity accelerates protein folding in the cell. FEBS Lett 377:505-511
    • (1995) FEBS Lett , vol.377 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 8
    • 43149088911 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • Hillson DA, Lambert N, Freedman RB (1984) Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol 48:487-492
    • (1984) Methods Enzymol , vol.48 , pp. 487-492
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 9
    • 0033974741 scopus 로고    scopus 로고
    • A protein disulfide isomerase gene fusion expression system that increase the extracellular productivity of Bacillus brevis
    • Kajino T, Ohto C, Muramatsu M, Obata S, Udaka S, Yamada Y, Takahashi H (2000) A protein disulfide isomerase gene fusion expression system that increase the extracellular productivity of Bacillus brevis. Appl Environ Microbiol Feb. 638-642
    • (2000) Appl Environ Microbiol , vol.FEB. , pp. 638-642
    • Kajino, T.1    Ohto, C.2    Muramatsu, M.3    Obata, S.4    Udaka, S.5    Yamada, Y.6    Takahashi, H.7
  • 12
    • 27644571313 scopus 로고    scopus 로고
    • Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system
    • Liu Y, Zhao T, Yan Y, Zhou H (2005) Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr Purif 44:155-161
    • (2005) Protein Expr Purif , vol.44 , pp. 155-161
    • Liu, Y.1    Zhao, T.2    Yan, Y.3    Zhou, H.4
  • 14
    • 0026416043 scopus 로고
    • Chaperon-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • 6330
    • Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl F-U (1991) Chaperon-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352(6330):36-42
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.-U.6
  • 16
    • 0025244292 scopus 로고
    • Purification and characterization of yeast protein disulfide isomerase
    • Mizunaga T, Katakura Y, Miura T, Maruyama Y (1990) Purification and characterization of yeast protein disulfide isomerase. J Biochem 108:846-851
    • (1990) J Biochem , vol.108 , pp. 846-851
    • Mizunaga, T.1    Katakura, Y.2    Miura, T.3    Maruyama, Y.4
  • 17
    • 16644374098 scopus 로고    scopus 로고
    • Establishment of a large-scale purification procedure for purified recombinant bovine interferon-τ produced by a silkworm-baculovirus gene expression system
    • Nagaya H, Kanaya T, Kaki H, Tobiya Y, Takahashi M, Takahashi H, Yokomizo Y, Inumaru S (2004) Establishment of a large-scale purification procedure for purified recombinant bovine interferon-τ produced by a silkworm-baculovirus gene expression system. J Vet Med Sci 66(11):1395-1401
    • (2004) J Vet Med Sci , vol.66 , Issue.11 , pp. 1395-1401
    • Nagaya, H.1    Kanaya, T.2    Kaki, H.3    Tobiya, Y.4    Takahashi, M.5    Takahashi, H.6    Yokomizo, Y.7    Inumaru, S.8
  • 18
    • 43149121980 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for the production of single-chain antibody fragment
    • Shusta EV, Rains RT, Pluckthum A, Wittrup KD (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for the production of single-chain antibody fragment. Nat Biotechnol 42:358-363
    • (1998) Nat Biotechnol , vol.42 , pp. 358-363
    • Shusta, E.V.1    Rains, R.T.2    Pluckthum, A.3    Wittrup, K.D.4
  • 19
    • 0025822385 scopus 로고
    • Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth
    • Tachikawa H, Miura T, Katakura Y, Mizunaga T (1991) Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth. J Biochem 110:306-313
    • (1991) J Biochem , vol.110 , pp. 306-313
    • Tachikawa, H.1    Miura, T.2    Katakura, Y.3    Mizunaga, T.4
  • 20
    • 28444432660 scopus 로고    scopus 로고
    • Expression of porcine lactorerrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization
    • 4
    • Wang Y, Wu X, Liu G, Cao C, Huang H, Xu Z, Liu J (2005) Expression of porcine lactorerrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization. Appl Microbiol Biotechnol 69(4):385-389
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 385-389
    • Wang, Y.1    Wu, X.2    Liu, G.3    Cao, C.4    Huang, H.5    Xu, Z.6    Liu, J.7
  • 21
    • 0037016671 scopus 로고    scopus 로고
    • Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
    • Winter J, Klappa P, Freedman RB, Lilie H, Rudolph R (2002) Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J Biol Chem 277:310-317
    • (2002) J Biol Chem , vol.277 , pp. 310-317
    • Winter, J.1    Klappa, P.2    Freedman, R.B.3    Lilie, H.4    Rudolph, R.5
  • 22
    • 33745049305 scopus 로고    scopus 로고
    • Expression of polyhedron-hEGF fusion protein in cultured cells and larvae of Bombyx mori
    • 11
    • Yu W, Chen J, Zhao X, Lv Z, Nie Z, Zhang Y (2006) Expression of polyhedron-hEGF fusion protein in cultured cells and larvae of Bombyx mori. Afr J Biotechnol 5(11):1034-1040
    • (2006) Afr J Biotechnol , vol.5 , pp. 1034-1040
    • Yu, W.1    Chen, J.2    Zhao, X.3    Lv, Z.4    Nie, Z.5    Zhang, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.