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Volumn 47, Issue 9, 2012, Pages 1364-1370

Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent

Author keywords

Mono PEGylation; PEGylation; Polyethylene glycol; Ribonuclease A; Thiolation

Indexed keywords

2-IMINOTHIOLANE; AMINO GROUP; ANALYTICAL CHARACTERIZATION; ANTI-PROLIFERATIVE; CANCER CHEMOTHERAPEUTIC AGENTS; ENZYMATIC ACTIVITIES; INDUSTRIAL PRODUCTION; MALEIMIDES; MONO-PEGYLATION; N-HYDROXYSUCCINIMIDE; PEGYLATED PROTEINS; PEGYLATION; PHARMACEUTICAL PRODUCTION; RIBONUCLEASE A; RNASE A; SOLVENT ACCESSIBILITY; THERAPEUTIC POTENTIALS; THERAPEUTIC PROTEIN; THIOL GROUPS; THIOLATION;

EID: 84862846674     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2012.05.003     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 0025412155 scopus 로고
    • Effects of monoethoxypoly(ethylene glycol) modification of ribonuclease on antibody recognition, substrate accessibility and conformational stability
    • P. Caliceti, O. Schiavon, F.M. Veronese, and I.M. Chaiken Effects of monoethoxypoly(ethylene glycol) modification of ribonuclease on antibody recognition, substrate accessibility and conformational stability J Mol Recognit 3 1990 89 93
    • (1990) J Mol Recognit , vol.3 , pp. 89-93
    • Caliceti, P.1    Schiavon, O.2    Veronese, F.M.3    Chaiken, I.M.4
  • 2
    • 36549004553 scopus 로고    scopus 로고
    • Anti-cancer PEG-enzymes: 30years old, but still a current approach
    • DOI 10.1016/j.addr.2007.04.018, PII S0169409X07001391, Peptide and Protein PEGylation III: Advances in Chemistry and Clinical Applications
    • G. Pasut, M. Sergi, and F.M. Veronese Anti-cancer PEG-enzyme: 30 years old, but still a current approach Adv Drug Deliv Rev 60 2008 69 78 (Pubitemid 350181167)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.1 , pp. 69-78
    • Pasut, G.1    Sergi, M.2    Veronese, F.M.3
  • 3
    • 38549168927 scopus 로고    scopus 로고
    • Ribonucleases as novel chemotherapeutics: The ranpirnase example
    • J.E. Lee, and R.T. Raines Ribonucleases as novel chemotherapeutics: the ranpiRNase A example BioDrugs 22 2008 53 58 (Pubitemid 351158535)
    • (2008) BioDrugs , vol.22 , Issue.1 , pp. 53-58
    • Lee, J.E.1    Raines, R.T.2
  • 4
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • DOI 10.1016/S0169-409X(02)00022-4, PII S0169409X02000224
    • M.J. Roberts, M.D. Bentley, and J.M. Harris Chemistry for peptide and protein PEGylation Adv Drug Deliv Rev 54 2002 459 476 (Pubitemid 34615543)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.4 , pp. 459-476
    • Roberts, M.J.1    Bentley, M.D.2    Harris, J.M.3
  • 5
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • DOI 10.1038/nrd1033
    • J.M. Harris, and R.B. Chess Effect of pegylation on pharmaceuticals Nat Rev Drug Discov 2 2003 214 221 (Pubitemid 37361666)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.3 , pp. 214-221
    • Milton Harris, J.1    Chess, R.B.2
  • 6
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • DOI 10.1016/S0142-9612(00)00193-9, PII S0142961200001939
    • F.M. Veronese Peptide and protein PEGylation: a review of problems and solutions Biomaterials 22 2001 405 417 (Pubitemid 32007845)
    • (2001) Biomaterials , vol.22 , Issue.5 , pp. 405-417
    • Veronese, F.M.1
  • 7
    • 78650539904 scopus 로고    scopus 로고
    • Ribonucleases of different origins with a wide spectrum of medicinal applications
    • E.F. Fang, and T.B. Ng Ribonucleases of different origins with a wide spectrum of medicinal applications Biochim Biophys Acta 1815 2011 65 74
    • (2011) Biochim Biophys Acta , vol.1815 , pp. 65-74
    • Fang, E.F.1    Ng, T.B.2
  • 8
    • 0026507445 scopus 로고
    • Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor
    • B.S. Murthy, and R. Sirdeshmukh Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor Biochem J 281 1992 343 348
    • (1992) Biochem J , vol.281 , pp. 343-348
    • Murthy, B.S.1    Sirdeshmukh, R.2
  • 9
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics
    • C.S. Fishburn The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics J Pharm Sci 97 2008 4167 4183
    • (2008) J Pharm Sci , vol.97 , pp. 4167-4183
    • Fishburn, C.S.1
  • 10
    • 0025783676 scopus 로고
    • Surface modification of enzymes for therapeutic use: Monomethoxypoly(ethylene glycol) derivatization of ribonuclease
    • O. Schiavon, P. Caliceri, L. Sartore, and F.M. Veronese Surface modification of enzymes for therapeutic use: monomethoxypoly(ethylene glycol) derivatization of ribonuclease Farmaco 46 1991 967 978
    • (1991) Farmaco , vol.46 , pp. 967-978
    • Schiavon, O.1    Caliceri, P.2    Sartore, L.3    Veronese, F.M.4
  • 12
    • 55749096038 scopus 로고    scopus 로고
    • PEGylation as a tool for the biomedical engineering of surface modified microparticles
    • U. Wattendorf, and H.P. Merkle PEGylation as a tool for the biomedical engineering of surface modified microparticles J Pharm Sci 97 2008 4655 4669
    • (2008) J Pharm Sci , vol.97 , pp. 4655-4669
    • Wattendorf, U.1    Merkle, H.P.2
  • 13
    • 3042722268 scopus 로고    scopus 로고
    • Protein, peptide and non-peptide drug PEGylation for therapeutic application
    • DOI 10.1517/13543776.14.6.859
    • G. Pasut, A. Guiotto, and F.M. Veronese Protein, peptide and non-peptide drug PEGylation for therapeutic application Expert Opin Ther Pat 14 2004 859 894 (Pubitemid 38868068)
    • (2004) Expert Opinion on Therapeutic Patents , vol.14 , Issue.6 , pp. 859-894
    • Pasut, G.1    Guiotto, A.2    Veronese, F.M.3
  • 14
    • 69849099305 scopus 로고    scopus 로고
    • A solid phase adsorption method for PEGylation of human serum albumin and staphylokinase: Preparation, purification and biochemical characterization
    • X. Suo, X. Lu, T. Hu, G. Ma, and Z. Su A solid phase adsorption method for PEGylation of human serum albumin and staphylokinase: preparation, purification and biochemical characterization Biotechnol Lett 31 2009 1191 1196
    • (2009) Biotechnol Lett , vol.31 , pp. 1191-1196
    • Suo, X.1    Lu, X.2    Hu, T.3    Ma, G.4    Su, Z.5
  • 15
    • 83655161394 scopus 로고    scopus 로고
    • An oriented adsorption strategy for efficient solid phase PEGylation of recombinant staphylokinase by immobilized metal-ion affinity chromatography
    • J. Wang, Y. Wang, T. Hu, X. Li, Y. Huang, and Y. Liu An oriented adsorption strategy for efficient solid phase PEGylation of recombinant staphylokinase by immobilized metal-ion affinity chromatography Process Biochem 47 2012 106 112
    • (2012) Process Biochem , vol.47 , pp. 106-112
    • Wang, J.1    Wang, Y.2    Hu, T.3    Li, X.4    Huang, Y.5    Liu, Y.6
  • 16
    • 27844515221 scopus 로고    scopus 로고
    • PEG-proteins: Reaction engineering and separation issues
    • C.J. Fee, and J.M. Van Alstine PEG-proteins: reaction engineering and separation issues Chem Eng Sci 61 2006 924 939
    • (2006) Chem Eng Sci , vol.61 , pp. 924-939
    • Fee, C.J.1    Van Alstine, J.M.2
  • 17
    • 0014487393 scopus 로고
    • Breakdown of doublestranded RNA by bull semen ribonuclease
    • M. Libonati, and A. Floridi Breakdown of doublestranded RNA by bull semen ribonuclease Eur J Biochem 8 1969 81 87
    • (1969) Eur J Biochem , vol.8 , pp. 81-87
    • Libonati, M.1    Floridi, A.2
  • 18
    • 0001483424 scopus 로고    scopus 로고
    • Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme
    • DOI 10.1046/j.1432-1327.1999.00761.x
    • G. Gotte, M. Bertoldi, and M. Libonati Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme Eur J Biochem 265 1999 680 687 (Pubitemid 29489001)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.2 , pp. 680-687
    • Gotte, G.1    Bertoldi, M.2    Libonati, M.3
  • 19
    • 33748536073 scopus 로고    scopus 로고
    • Natural and engineered ribonucleases as potential cancer therapeutics
    • DOI 10.1007/s10529-006-9145-0
    • U. Arnold, and R. Ulbrich-Hofmann Natural and engineered ribonucleases as potential cancer therapeutics Biotechnol Lett 28 2006 1615 1622 (Pubitemid 44369323)
    • (2006) Biotechnology Letters , vol.28 , Issue.20 , pp. 1615-1622
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 20
    • 0036290272 scopus 로고    scopus 로고
    • Preparation of well-defined bovine polyhemoglobin based on dimethyl adipimidate and glutaraldebyde cross-linkage
    • DOI 10.1016/S0006-291X(02)00310-8, PII S0006291X02003108
    • T. Hu, and Z. Su Preparation of well-defined polyhemoglobin based on dimethyl apidimidate and glutaraldehyde cross-linkage Biochem Biophys Res Commun 293 2002 958 961 (Pubitemid 34694134)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.3 , pp. 958-961
    • Hu, T.1    Su, Z.2
  • 22
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assay
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assay J Immunol Methods 65 1983 55 62
    • (1983) J Immunol Methods , vol.65 , pp. 55-62
    • Mosmann, T.1
  • 24
    • 33846969212 scopus 로고    scopus 로고
    • Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin
    • T. Hu, B.N. Manjula, D. Li, M. Brenowitz, and A.S. Acharya Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin Biochem J 402 2007 143 151
    • (2007) Biochem J , vol.402 , pp. 143-151
    • Hu, T.1    Manjula, B.N.2    Li, D.3    Brenowitz, M.4    Acharya, A.S.5
  • 25
    • 0024093648 scopus 로고    scopus 로고
    • Effect of sulfitolysis of disulfide bonds of bovine serum albumin on its structual properties: A physicochemical study
    • N.K. Kella, Y. Kang, and J.E. Kinsella Effect of sulfitolysis of disulfide bonds of bovine serum albumin on its structual properties: a physicochemical study J Protein Chem 7 1998 535 548
    • (1998) J Protein Chem , vol.7 , pp. 535-548
    • Kella, N.K.1    Kang, Y.2    Kinsella, J.E.3
  • 26
    • 55449120745 scopus 로고    scopus 로고
    • Effect of Ethylene Glycol and Polyethylene Glycol on the Acid-Unfolded State of Trypsinogen
    • DOI 10.1023/B:JOPC.0000008733.93463.ed
    • F. Naseemand, and R.H. Khan Effect of ethylene glycol and polyethylene glycol on the acid-unfolded state of trypsinogen J Protein Chem 22 2003 677 682 (Pubitemid 38036731)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.7-8 , pp. 677-682
    • Naseem, F.1    Khan, R.H.2
  • 27
  • 28
    • 0035965873 scopus 로고    scopus 로고
    • X-Ray and neutron scattering analyses of hydration shells: A molecular interpretation based on sequence predictions and modelling fits
    • DOI 10.1016/S0301-4622(01)00216-2, PII S0301462201002162
    • S.J. Perkins X-ray and neutron scattering analyses of hydration shells: a molecular interpretation based on sequence predictions and modelling fits Biophys Chem 93 2001 129 139 (Pubitemid 34142182)
    • (2001) Biophysical Chemistry , vol.93 , Issue.2-3 , pp. 129-139
    • Perkins, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.