Activation of a refolded, berberine-specific, single-chain Fv fragment by addition of free berberine

Biotechnology Letters

Volumn 28, Issue 13, 2006, Pages 999-1006

  Kim, Jun Sik ^a   Masaki, Tadashi ^b   Sirikantaramas, Supaart ^b   Shoyama, Yukihiro ^b   Tanaka, Hiroyuki ^b  

^a Dongshin University   (South Korea)

^b KYUSHU UNIVERSITY   (Japan)

Author keywords

Artificial chaperone; Berberine; ELISA; Inclusion body; Refolding; scFvs

Indexed keywords

ARTIFICIAL CHAPERONE; BERBERINE; ELISA; INCLUSION BODY; REFOLDING; SCFVS;

ANTIBODIES; BIOASSAY; CLONING; DIALYSIS; ENZYMES; GENES;

PLANTS (BOTANY);

BERBERINE; MONOCLONAL ANTIBODY;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; CELL LINE; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENETICS; HUMAN; HYBRIDOMA; IMMUNOGLOBULIN VARIABLE REGION; IMMUNOLOGY; METABOLISM; METHODOLOGY; MOUSE; PROTEIN ENGINEERING; PROTEIN FOLDING;

ANIMALS; ANTIBODIES, MONOCLONAL; BERBERINE; CELL LINE; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; HUMANS; HYBRIDOMAS; IMMUNOGLOBULIN VARIABLE REGION; MICE; MICE, INBRED BALB C; PROTEIN ENGINEERING; PROTEIN FOLDING;

ESCHERICHIA COLI;

EID: 33745711978     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-006-9033-7     Document Type: Article

References (19)

1. Bilbao G, Contreras JL, Curiel DT (2002) Genetically engineered intracellular single-chain antibodies in gene therapy. Mol Biotechnol 22:191-211
2. Buchner J, Pastan I, Brinkmann U (1992) A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal Biochem 205:263-270
3. Fra AM, Fagioli C, Finazzi D, Sitia R, Alberini CM (1993) Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J 12:4755-4761
4. Jäger M, Plünckthun A (1999) Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen. J Mol Biol 285:2005-2019
5. Kabat EA, Wu TT, Perry HM, Gottensman K, Foeller C (1997) Sequences of proteins of immunological interest. NIH, Bethesda
6. Knappik A, Plünckthun A (1995) Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng 8:81-89
7. Kim JS, Tanaka H, Shoyama Y (2004a) Immunoquantitative analysis for berberine and its related compounds using monoclonal antibodies in herbal medicines. Analyst 129:87-91
8. Kim JS, Tanaka H, Yuan CS, Shoyama Y (2004b) Development of monoclonal antibody against isoquinoline alkaloid coptisine and its application for the screening of medicinal plants. Cytotechnology 44:115-123
9. Machida S, Ogawa S, Shi X, Takaha T, Fujii K, Hayashi K (2000) Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett 486:131-135
10. Proba K, Honegger A, Plückthun A (1997) A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding. J Mol Biol 265:161-172
11. Ramm K, Gehrig P, Plückthun A (1999) Removal of the conserved disulfide bridges from the scFv fragment of an antibody: effects on folding kinetics and aggregation. J Mol Biol 290:535-546
12. Reiter Y, Pastan I (1996) Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins. Clin Cancer Res 2:245-252
13. Schmiedl A, Breitling F, Winter CH, Queitsch I, Dübel S (2000) Effects of unpaired cysteines on yield, solubility and activity of different recombinant antibody constructs expressed in E. coli. J Immunol Methods 242:101-114
14. Sitia R, Neuberger M, Alberini C, Bet P, Fra A, Valetti C (1990) Developmental regulation of IgM secretion: the role of the carboxy-terminal cysteine. Cell 60:781-790
15. Shoyama Y, Tanaka H, Fukuda N (1999) Monoclonal antibodies against naturally occurring bioactive compounds. Cytotechnology 31:9-27
16. Sedlak J, Lindsay RH (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal Biochem 25:192-205
17. Todorovska A, Roovers RC, Dolezal O, Kortt AA, Hoogenboom HR, Hudson PJ (2001) Design and application of diabodies, triabodies and tetrabodies for cancer targeting. J Immunol Methods 248:47-66
18. Umetsu M, Tsumoto K, Hara M, Ashish K, Goda S, Adschiri T, Kumagai I (2003) How additives influence the refolding of immunoglobulin-folded proteins in stepwise dialysis system. J Biol Chem 278:8979-8987
19. Yokota T, Milenic DE, Whitlow M, Schlom J (1992) Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res 52:3402-3408