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Volumn 65, Issue 1, 2009, Pages 105-109

Separation of PEGylated from unmodified ribonuclease A using sepharose media

Author keywords

Chromatography media development; PEGylated proteins; Ribonuclease A

Indexed keywords

AMMONIUM COMPOUNDS; ANIMAL CELL CULTURE; CHROMATOGRAPHIC ANALYSIS; CHROMATOGRAPHY; ENZYMES; GEL PERMEATION CHROMATOGRAPHY; IONIC STRENGTH; PH; PHASE SEPARATION; PHOSPHATES; POLYETHYLENE GLYCOLS; PROTEINS; SEPARATION;

EID: 58149288080     PISSN: 13835866     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.seppur.2008.10.038     Document Type: Article
Times cited : (36)

References (18)
  • 1
    • 17844380498 scopus 로고    scopus 로고
    • Pegylation: a novel process for modifying pharmacokinetics
    • Harris J.M., Martin N.E., and Modi M. Pegylation: a novel process for modifying pharmacokinetics. Clin. Pharmacokinet. 40 (2001) 539-551
    • (2001) Clin. Pharmacokinet. , vol.40 , pp. 539-551
    • Harris, J.M.1    Martin, N.E.2    Modi, M.3
  • 2
    • 0036188810 scopus 로고    scopus 로고
    • Coupling of the antitumoral enzyme bovine seminal ribonuclease to polyethylene glycol chains increases its systemic efficacy in mice
    • Michaelis M., Cinatl J., Pouckova P., Langer K., Kreuter J., and Matousek J. Coupling of the antitumoral enzyme bovine seminal ribonuclease to polyethylene glycol chains increases its systemic efficacy in mice. Anti-Cancer Drugs 13 (2002) 149-154
    • (2002) Anti-Cancer Drugs , vol.13 , pp. 149-154
    • Michaelis, M.1    Cinatl, J.2    Pouckova, P.3    Langer, K.4    Kreuter, J.5    Matousek, J.6
  • 3
    • 0029360545 scopus 로고
    • Chemistry of polyethylene glycol conjugates with biologically active molecules
    • Zalipsky S. Chemistry of polyethylene glycol conjugates with biologically active molecules. Adv. Drug Deliv. Rev. 16 (1995) 157-182
    • (1995) Adv. Drug Deliv. Rev. , vol.16 , pp. 157-182
    • Zalipsky, S.1
  • 4
    • 27844515221 scopus 로고    scopus 로고
    • PEG-proteins: reaction engineering and separation issues
    • Fee C.J., and Van Alstine J.M. 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
  • 5
    • 0035951339 scopus 로고    scopus 로고
    • Use of ion-exchange chromatography and hydrophobic interaction chromatography in the preparation and recovery of polyethylene glycol-linked proteins
    • Seely J.E., and Richey C.W. Use of ion-exchange chromatography and hydrophobic interaction chromatography in the preparation and recovery of polyethylene glycol-linked proteins. J. Chromatogr. A 908 (2001) 235-241
    • (2001) J. Chromatogr. A , vol.908 , pp. 235-241
    • Seely, J.E.1    Richey, C.W.2
  • 7
    • 0000031014 scopus 로고    scopus 로고
    • A comparison of polystyrene-poly(ethylene oxide) diblock copolymer and poly(ethylene oxide) homopolymer adsorption from aqueous solutions
    • Pagac E.S., Prieve D.C., Solomentsev Y., and Tilton R.D. A comparison of polystyrene-poly(ethylene oxide) diblock copolymer and poly(ethylene oxide) homopolymer adsorption from aqueous solutions. Langmuir 13 (1997) 2993-3001
    • (1997) Langmuir , vol.13 , pp. 2993-3001
    • Pagac, E.S.1    Prieve, D.C.2    Solomentsev, Y.3    Tilton, R.D.4
  • 8
    • 19544388245 scopus 로고    scopus 로고
    • Prediction of protein retention in hydrophobic interaction chromatography
    • Mahn A., and Asenjo J.A. Prediction of protein retention in hydrophobic interaction chromatography. Biotechnol. Adv. 23 (2005) 359-368
    • (2005) Biotechnol. Adv. , vol.23 , pp. 359-368
    • Mahn, A.1    Asenjo, J.A.2
  • 9
    • 0035805436 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins
    • Queiroz J.A., Tomaz C.T., and Cabral J.M.S. Hydrophobic interaction chromatography of proteins. J. Biotechnol. 87 (2001) 143-159
    • (2001) J. Biotechnol. , vol.87 , pp. 143-159
    • Queiroz, J.A.1    Tomaz, C.T.2    Cabral, J.M.S.3
  • 10
    • 0037130163 scopus 로고    scopus 로고
    • PEG chains increase aspermatogenic and antitumor activity of RNase A and BS-RNase enzyme
    • Matousek J., Pouckova P., Soucek J., and Skvor J. PEG chains increase aspermatogenic and antitumor activity of RNase A and BS-RNase enzyme. J. Control. Release 82 (2002) 29-37
    • (2002) J. Control. Release , vol.82 , pp. 29-37
    • Matousek, J.1    Pouckova, P.2    Soucek, J.3    Skvor, J.4
  • 11
    • 19944380795 scopus 로고    scopus 로고
    • Adsorption of poly(ethylene glycol)-modified ribonuclease A to a poly(lactide-co-glycolide) surface
    • Daly S.M., Przybycien T.M., and Tilton R.D. Adsorption of poly(ethylene glycol)-modified ribonuclease A to a poly(lactide-co-glycolide) surface. Biotechnol. Bioeng. 90 (2005) 856-868
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 856-868
    • Daly, S.M.1    Przybycien, T.M.2    Tilton, R.D.3
  • 12
    • 0024315152 scopus 로고
    • Polyoxyalkyleneglycols immobilized on sepharose 6B for the sequential extraction of three enzymes from a crude extract of Pseudomonas testosterone
    • Mathis R., Hubert P., and Dellacherie E. Polyoxyalkyleneglycols immobilized on sepharose 6B for the sequential extraction of three enzymes from a crude extract of Pseudomonas testosterone. J. Chromatrogr. 474 (1989) 396-399
    • (1989) J. Chromatrogr. , vol.474 , pp. 396-399
    • Mathis, R.1    Hubert, P.2    Dellacherie, E.3
  • 13
    • 0029933936 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of Chromobacterium viscosum lipase on polyethylene glycol immobilized on sepharose
    • Queiroz J.A., Garcia F.A.P., and Cabral J.M.S. Hydrophobic interaction chromatography of Chromobacterium viscosum lipase on polyethylene glycol immobilized on sepharose. J. Chromatrogr. A 734 (1996) 213-219
    • (1996) J. Chromatrogr. A , vol.734 , pp. 213-219
    • Queiroz, J.A.1    Garcia, F.A.P.2    Cabral, J.M.S.3
  • 14
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines R. Ribonuclease A. Chem. Rev. 98 (1998) 1045-1065
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.1
  • 16
    • 0025874085 scopus 로고
    • Adsorption-desorption isotherm hysteresis of β-lactoglobulin A with a weakly hydrophobic surface
    • Lin S., Blanco R., and Karger B.L. Adsorption-desorption isotherm hysteresis of β-lactoglobulin A with a weakly hydrophobic surface. J. Chromatogr. 557 (1991) 369-382
    • (1991) J. Chromatogr. , vol.557 , pp. 369-382
    • Lin, S.1    Blanco, R.2    Karger, B.L.3
  • 17
    • 22244432520 scopus 로고    scopus 로고
    • Adsorption isotherms and irreversible binding of proteins on commercially available hydrophobic adsorbents
    • Millitzer M., Wenzig E., and Peukert W. Adsorption isotherms and irreversible binding of proteins on commercially available hydrophobic adsorbents. Chem. Eng. Technol. 28 (2005) 756-761
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 756-761
    • Millitzer, M.1    Wenzig, E.2    Peukert, W.3
  • 18
    • 21344449279 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography: harnessing multivalent protein-surface interactions for purification procedures
    • Jennissen H.P. Hydrophobic interaction chromatography: harnessing multivalent protein-surface interactions for purification procedures. Methods Mol. Biol. 305 (2005) 81-99
    • (2005) Methods Mol. Biol. , vol.305 , pp. 81-99
    • Jennissen, H.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.