메뉴 건너뛰기




Volumn 14, Issue 1, 1998, Pages 104-112

Expression, purification, and characterization of recombinant ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit N(ε)-methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CDNA LIBRARY; CELL CULTURE; CHLOROPLAST; ENZYME ACTIVITY; HOMOGENEITY; METHYLATION; METHYLTRANSFERASE; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; PHOTOSYNTHESIS; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 0032190317     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0936     Document Type: Article
Times cited : (25)

References (18)
  • 2
    • 0000196404 scopus 로고
    • Protection of tryptic-sensitive sites in the large subunit of ribulose bisphosphate carboxylase/oxygenase by catalysis
    • Houtz R. L., Mulligan R. M. Protection of tryptic-sensitive sites in the large subunit of ribulose bisphosphate carboxylase/oxygenase by catalysis. Plant Physiol. 96:1991;335-339.
    • (1991) Plant Physiol. , vol.96 , pp. 335-339
    • Houtz, R.L.1    Mulligan, R.M.2
  • 3
    • 0023971857 scopus 로고
    • Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: The amino-terminal residue of the large subunit is acetylated proline
    • Mulligan R. M., Houtz R. L., Tolbert N. E. Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: The amino-terminal residue of the large subunit is acetylated proline. Proc. Natl. Acad. Sci. USA. 85:1988;1513-1517.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1513-1517
    • Mulligan, R.M.1    Houtz, R.L.2    Tolbert, N.E.3
  • 4
    • 0024636180 scopus 로고
    • Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase
    • Houtz R. L., Stults J. T., Mulligan R. M., Tolbert N. E. Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase. Proc. Natl. Acad. Sci. USA. 86:1989;1855-1859.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1855-1859
    • Houtz, R.L.1    Stults, J.T.2    Mulligan, R.M.3    Tolbert, N.E.4
  • 5
    • 0001067511 scopus 로고
    • Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species
    • Houtz R. L., Poneleit L., Jones S. B., Royer M., Stults J. T. Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species. Plant Physiol. 98:1992;1170-1174.
    • (1992) Plant Physiol. , vol.98 , pp. 1170-1174
    • Houtz, R.L.1    Poneleit, L.2    Jones, S.B.3    Royer, M.4    Stults, J.T.5
  • 8
    • 0029169542 scopus 로고
    • Cloning and developmental expression of pea ribulose-1,5-bisphosphate carboxylase/oxygenase large subunitN
    • Klein R. R., Houtz R. L. Cloning and developmental expression of pea ribulose-1,5-bisphosphate carboxylase/oxygenase large subunitN. Plant Mol. Biol. 27:1995;249-261.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 249-261
    • Klein, R.R.1    Houtz, R.L.2
  • 10
    • 0020348141 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach, tomato or tobacco leaves
    • McCurry S. D., Gee R., Tolbert N. E. Ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach, tomato or tobacco leaves. Methods Enzymol. 90:1982;515-521.
    • (1982) Methods Enzymol. , vol.90 , pp. 515-521
    • McCurry, S.D.1    Gee, R.2    Tolbert, N.E.3
  • 12
    • 0004167692 scopus 로고
    • Novagen, Inc. Novagen, Inc. Madison, WI
    • Novagen, Inc. 1995, pET System Manual, Novagen, Inc. Madison, WI.
    • (1995) Pet System Manual
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-255.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-255
    • Bradford, M.M.1
  • 14
    • 0000813771 scopus 로고
    • Partial purification and characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit ςn
    • Houtz R. L., Royer M., Salvucci M. E. Partial purification and characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit ςN. Plant Physiol. 97:1991;913-920.
    • (1991) Plant Physiol. , vol.97 , pp. 913-920
    • Houtz, R.L.1    Royer, M.2    Salvucci, M.E.3
  • 16
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 17
    • 0025975025 scopus 로고
    • Cleavage of the precursor of pea chloroplast cytochrome f by leader peptidase fromEscherichia coli.
    • Anderson C. M., Gray J. Cleavage of the precursor of pea chloroplast cytochrome f by leader peptidase fromEscherichia coli. FEBS Lett. 280:1991;383-386.
    • (1991) FEBS Lett. , vol.280 , pp. 383-386
    • Anderson, C.M.1    Gray, J.2
  • 18
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea-seed ferritins expressed inEscherichia coli:in vitro.
    • van Wuytswinkel O., Savino G., Briat J.-F. Purification and characterization of recombinant pea-seed ferritins expressed inEscherichia coli:in vitro. Biochem. J. 305:1995;253-261.
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • Van Wuytswinkel, O.1    Savino, G.2    Briat, J.-F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.