메뉴 건너뛰기




Volumn 14, Issue 1, 1998, Pages 139-145

Purification of active chloroplast sedoheptulose-1,7-bisphosphatase expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPLAST; ENZYME PURIFICATION; SEDOHEPTULOSE 1,7 BISPHOSPHATASE;

EID: 0032190590     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0939     Document Type: Article
Times cited : (17)

References (26)
  • 1
    • 0003374644 scopus 로고
    • Fructose-1,6-bisphosphatase form B fromSynechococcus leopoliensis
    • Gerbling K-P., Steup M., Latzko E. Fructose-1,6-bisphosphatase form B fromSynechococcus leopoliensis. Plant Physiol. 80:1986;716-720.
    • (1986) Plant Physiol. , vol.80 , pp. 716-720
    • Gerbling, K-P.1    Steup, M.2    Latzko, E.3
  • 2
    • 0017850750 scopus 로고
    • Chloroplast sedoheptulose-1,7-bisphosphatase: Evidence for regulation by the ferredoxin/thioredoxin system
    • Breazeale V. D., Buchanan B. B., Wolosiuk R. A. Chloroplast sedoheptulose-1,7-bisphosphatase: Evidence for regulation by the ferredoxin/thioredoxin system. Z. Naturforsch. 33C:1978;521-528.
    • (1978) Z. Naturforsch. , vol.33 , pp. 521-528
    • Breazeale, V.D.1    Buchanan, B.B.2    Wolosiuk, R.A.3
  • 4
    • 0023085955 scopus 로고
    • Isolation and purification of chloroplastic spinach (Spinacia oleracea
    • Cadet F., Meunier J-C., Ferté N. Isolation and purification of chloroplastic spinach (Spinacia oleracea. Biochem. J. 241:1987;71-74.
    • (1987) Biochem. J. , vol.241 , pp. 71-74
    • Cadet, F.1    Meunier, J-C.2    Ferté, N.3
  • 5
    • 0026557817 scopus 로고
    • CDNA and gene sequences of wheat chloroplastic sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphatases
    • Raines C. A., Lloyd J. C., Willingham N. M., Potts S., Dyer T. A. cDNA and gene sequences of wheat chloroplastic sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphatases. Eur. J. Biochem. 205:1992;1053-1059.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1053-1059
    • Raines, C.A.1    Lloyd, J.C.2    Willingham, N.M.3    Potts, S.4    Dyer, T.A.5
  • 9
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan B. B. Role of light in the regulation of chloroplast enzymes. Annu. Rev. Plant Physiol. 31:1980;341-374.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 10
    • 12044250534 scopus 로고
    • Redox-modulation of chloroplast enzymes. A common principle for individual control
    • Scheibe R. Redox-modulation of chloroplast enzymes. A common principle for individual control. Plant Physiol. 96:1991;1-3.
    • (1991) Plant Physiol. , vol.96 , pp. 1-3
    • Scheibe, R.1
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0031929442 scopus 로고    scopus 로고
    • Reduced sedoheptulose-1,7-bisphosphatase levels in transgenic tobacco lead to decreased photosynthetic capacity and altered carbohydrate accumulation
    • Harrison E. P., Willingham N. M., Lloyd J. C., Raines C. A. Reduced sedoheptulose-1,7-bisphosphatase levels in transgenic tobacco lead to decreased photosynthetic capacity and altered carbohydrate accumulation. Planta. 204:1998;27-36.
    • (1998) Planta , vol.204 , pp. 27-36
    • Harrison, E.P.1    Willingham, N.M.2    Lloyd, J.C.3    Raines, C.A.4
  • 15
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • Gavel Y., von Heijne G. A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261:1990;455-458.
    • (1990) FEBS Lett. , vol.261 , pp. 455-458
    • Gavel, Y.1    Von Heijne, G.2
  • 16
    • 0027410046 scopus 로고
    • The pRSET family of T7 promoter expression vectors forEscherichia coli.
    • Schoepfer R. The pRSET family of T7 promoter expression vectors forEscherichia coli. Gene. 124:1993;83-85.
    • (1993) Gene , vol.124 , pp. 83-85
    • Schoepfer, R.1
  • 17
    • 0021010765 scopus 로고
    • Purification and partial amino acid sequence analysis of the cellular tumour antigen, p53, from mouse SV40-transformed cells
    • Leppard K., Totty N., Waterfield M., Harlow E., Jenkins J., Crawford L. Purification and partial amino acid sequence analysis of the cellular tumour antigen, p53, from mouse SV40-transformed cells. EMBO J. 2:1983;1993-1999.
    • (1983) EMBO J. , vol.2 , pp. 1993-1999
    • Leppard, K.1    Totty, N.2    Waterfield, M.3    Harlow, E.4    Jenkins, J.5    Crawford, L.6
  • 18
    • 0026327753 scopus 로고
    • A novel strategy for production of highly expressed recombinant protein in an active form
    • Blackwell J. R., Horgan R. A novel strategy for production of highly expressed recombinant protein in an active form. FEBS Lett. 295:1993;10-12.
    • (1993) FEBS Lett. , vol.295 , pp. 10-12
    • Blackwell, J.R.1    Horgan, R.2
  • 21
    • 0026134778 scopus 로고
    • Effect of ethanol and low-temperature culture on expression of soybean lipoxygenase L-1 inEscherichia coli.
    • Steczko J., Donoho G. A., Dixon J. E., Sugimoto T., Axelrod B. Effect of ethanol and low-temperature culture on expression of soybean lipoxygenase L-1 inEscherichia coli. Protein Expression Purif. 2:1991;221-227.
    • (1991) Protein Expression Purif. , vol.2 , pp. 221-227
    • Steczko, J.1    Donoho, G.A.2    Dixon, J.E.3    Sugimoto, T.4    Axelrod, B.5
  • 22
    • 15844395096 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body formation in recombinantEscherichia coli
    • Thomas J. G., Baneyx F. Protein misfolding and inclusion body formation in recombinantEscherichia coli. J. Biol. Chem. 271:1996;11141-11147.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Baneyx, F.2
  • 23
    • 0020164171 scopus 로고
    • Activation of wheat chloroplast sedoheptulose bisphosphatase: A continuous spectrophotometric assay
    • Woodrow I. E., Walker D. A. Activation of wheat chloroplast sedoheptulose bisphosphatase: A continuous spectrophotometric assay. Arch. Biochem. Biophys. 216:1982;416-422.
    • (1982) Arch. Biochem. Biophys. , vol.216 , pp. 416-422
    • Woodrow, I.E.1    Walker, D.A.2
  • 24
    • 0027173978 scopus 로고
    • Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ
    • Süss K.-H., Arkona C., Manteuffel R., Adler K. Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proc. Natl. Acad. Sci. USA. 90:1993;5514-5518.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5514-5518
    • Süss, K.-H.1    Arkona, C.2    Manteuffel, R.3    Adler, K.4
  • 25
    • 0027223248 scopus 로고
    • Electron-microscopical localisation of chloroplast proteins by immunogold labelling on cryo-embedded spinach leaves
    • Adler K., Arkona C., Manteuffel R., Süss K.-H. Electron-microscopical localisation of chloroplast proteins by immunogold labelling on cryo-embedded spinach leaves. Cell Biol. Int. 17:1993;213-220.
    • (1993) Cell Biol. Int. , vol.17 , pp. 213-220
    • Adler, K.1    Arkona, C.2    Manteuffel, R.3    Süss, K.-H.4
  • 26
    • 0030454774 scopus 로고    scopus 로고
    • Distribution of ten enzymes of carbon metabolism in pea (Pisum sativum
    • Anderson L. E., Gibbons J. T., Wang X. Distribution of ten enzymes of carbon metabolism in pea (Pisum sativum. Int. J. Plant Sci. 157:1996;525-538.
    • (1996) Int. J. Plant Sci. , vol.157 , pp. 525-538
    • Anderson, L.E.1    Gibbons, J.T.2    Wang, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.