메뉴 건너뛰기




Volumn 382, Issue 1, 2008, Pages 66-68

Free sulfhydryl measurement as an indicator of antibody stability

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODIES; THERMODYNAMIC STABILITY;

EID: 51249120701     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.07.016     Document Type: Article
Times cited : (59)

References (16)
  • 1
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow E., and Lane D. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 2
    • 0031575401 scopus 로고    scopus 로고
    • A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding
    • Proba K., Honegger A., and Pluckthun A. A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding. J. Mol. Biol. 265 (1997) 161-172
    • (1997) J. Mol. Biol. , vol.265 , pp. 161-172
    • Proba, K.1    Honegger, A.2    Pluckthun, A.3
  • 3
    • 0022519389 scopus 로고
    • Reduction of the buried intrachain disulfide bond of the constant fragment of the immunoglobulin light chain: global unfolding under physiological conditions
    • Kikuchi H., Goto Y., and Hamaguchi K. Reduction of the buried intrachain disulfide bond of the constant fragment of the immunoglobulin light chain: global unfolding under physiological conditions. Biochemistry 25 (1986) 2009-2013
    • (1986) Biochemistry , vol.25 , pp. 2009-2013
    • Kikuchi, H.1    Goto, Y.2    Hamaguchi, K.3
  • 4
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 5
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Worn A., and Pluckthun A. Stability engineering of antibody single-chain Fv fragments. J. Mol. Biol. 305 (2001) 989-1010
    • (2001) J. Mol. Biol. , vol.305 , pp. 989-1010
    • Worn, A.1    Pluckthun, A.2
  • 6
    • 0031302744 scopus 로고    scopus 로고
    • X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain
    • Uson I., Bes M.T., Sheldrick G.M., Schneider T.R., Hartsch T., and Fritz H.-J. X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain. Folding Design 2 (1997) 357-361
    • (1997) Folding Design , vol.2 , pp. 357-361
    • Uson, I.1    Bes, M.T.2    Sheldrick, G.M.3    Schneider, T.R.4    Hartsch, T.5    Fritz, H.-J.6
  • 7
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds, made by molecular evolution
    • Proba K., Worn A., Honegger A., and Pluckthun A. Antibody scFv fragments without disulfide bonds, made by molecular evolution. J. Mol. Biol. 275 (1998) 245-253
    • (1998) J. Mol. Biol. , vol.275 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Pluckthun, A.4
  • 8
    • 0035988060 scopus 로고    scopus 로고
    • Free sulfhydryl in recombinant monoclonal antibodies
    • Zhang W., and Czupryn M.J. Free sulfhydryl in recombinant monoclonal antibodies. Biotechnol. Prog. 18 (2002) 509-513
    • (2002) Biotechnol. Prog. , vol.18 , pp. 509-513
    • Zhang, W.1    Czupryn, M.J.2
  • 10
    • 34047270107 scopus 로고    scopus 로고
    • A role for protein misfolding in immunogenicity of biopharmaceuticals
    • Maas C., Hermeling S., Bouma B., Jiskoot W., and Gebbink M.F.B.G. A role for protein misfolding in immunogenicity of biopharmaceuticals. J. Biol. Chem. 282 (2007) 2229-2236
    • (2007) J. Biol. Chem. , vol.282 , pp. 2229-2236
    • Maas, C.1    Hermeling, S.2    Bouma, B.3    Jiskoot, W.4    Gebbink, M.F.B.G.5
  • 12
    • 0027528596 scopus 로고
    • Comparison of Ellman's reagent with N-(1-pyrenyl)maleimide for the determination of free sulfhydryl groups in reduced cellobiohydrolase I from Trichoderma reesei
    • Woodward J., Tate J., Herrmann P.C., and Evans B.R. Comparison of Ellman's reagent with N-(1-pyrenyl)maleimide for the determination of free sulfhydryl groups in reduced cellobiohydrolase I from Trichoderma reesei. J. Biochem. Biophys. Methods 26 (1993) 121-129
    • (1993) J. Biochem. Biophys. Methods , vol.26 , pp. 121-129
    • Woodward, J.1    Tate, J.2    Herrmann, P.C.3    Evans, B.R.4
  • 13
    • 0029026590 scopus 로고
    • Analysis of glutathione, glutathione disulfide, cysteine, homocysteine, and other biological thiols by high-performance liquid chromatography following derivatization by N-(1-pyrenyl) maleimide
    • Winters R.A., Zukowski J., Ercal N., Matthews R.H., and Spitz D.R. Analysis of glutathione, glutathione disulfide, cysteine, homocysteine, and other biological thiols by high-performance liquid chromatography following derivatization by N-(1-pyrenyl) maleimide. Anal. Biochem. 227 (1995) 14-21
    • (1995) Anal. Biochem. , vol.227 , pp. 14-21
    • Winters, R.A.1    Zukowski, J.2    Ercal, N.3    Matthews, R.H.4    Spitz, D.R.5
  • 14
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry S., Mandelkow H., Brick P., and Franks N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5 (1998) 827-835
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 15
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He X.M., and Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 358 (1992) 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 16
    • 0035041251 scopus 로고    scopus 로고
    • The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study
    • Ferrer M.L., Duchowicz R., Carrasco B., de la Torre J.G., and Acuna A.U. The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophys. J. 80 (2001) 2422-2430
    • (2001) Biophys. J. , vol.80 , pp. 2422-2430
    • Ferrer, M.L.1    Duchowicz, R.2    Carrasco, B.3    de la Torre, J.G.4    Acuna, A.U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.