메뉴 건너뛰기




Volumn 90, Issue 3, 2005, Pages 380-390

Correlation for the partition behavior of proteins in aqueous two-phase systems: Effect of surface hydrophobicity and charge

Author keywords

Aqueous two phase systems; Charge density; Correlation for partition coefficient; Hydrophobicity; Precipitation

Indexed keywords

CARRIER CONCENTRATION; CONCENTRATION (PROCESS); ELECTROPHORESIS; HYDROPHOBICITY; POLYETHYLENE GLYCOLS; SODIUM CHLORIDE; SOLUBILITY; SOLUTIONS; SURFACE PHENOMENA; TITRATION; TWO PHASE FLOW;

EID: 20344402070     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20495     Document Type: Article
Times cited : (152)

References (37)
  • 3
    • 0028241249 scopus 로고
    • Model for predicting the partition behaviour of proteins in aqueous two-phase systems
    • Asenjo JA, Schmidt AS, Hachem F, Andrews BA. 1994. Model for predicting the partition behaviour of proteins in aqueous two-phase systems. J Chromatogr 668:47-54.
    • (1994) J Chromatogr , vol.668 , pp. 47-54
    • Asenjo, J.A.1    Schmidt, A.S.2    Hachem, F.3    Andrews, B.A.4
  • 4
    • 0030435453 scopus 로고    scopus 로고
    • Partitioning and purification of monoclonal antibodies in aqueous two-phase systems
    • Asenjo JA, Nielsen S, Andrews BA. 1996. Partitioning and purification of monoclonal antibodies in aqueous two-phase systems. Bioseparation 6:303-313.
    • (1996) Bioseparation , vol.6 , pp. 303-313
    • Asenjo, J.A.1    Nielsen, S.2    Andrews, B.A.3
  • 5
    • 0011366552 scopus 로고
    • Thermodynamics of separation of biomaterials in two-phase aqueous polymer systems: Effect of the phase-forming polymers
    • Baskir JN, Hatton TA, Suter UW. 1987. Thermodynamics of separation of biomaterials in two-phase aqueous polymer systems: effect of the phase-forming polymers. Macromolecules 20:1300-1311.
    • (1987) Macromolecules , vol.20 , pp. 1300-1311
    • Baskir, J.N.1    Hatton, T.A.2    Suter, U.W.3
  • 6
    • 0025526357 scopus 로고
    • Statistical thermodynamics of phase separation and ion partitioning in aqueous two-phase systems
    • Cabezas HJ, Kabiri-Badr M, Szlag DC. 1990. Statistical thermodynamics of phase separation and ion partitioning in aqueous two-phase systems. Bioseparation 1:227-233.
    • (1990) Bioseparation , vol.1 , pp. 227-233
    • Cabezas, H.J.1    Kabiri-Badr, M.2    Szlag, D.C.3
  • 7
    • 0026203774 scopus 로고
    • Partitioning and purification of thaumatin in aqueous two-phase systems
    • Cascone O, Andrews BA, Asenjo JA. 1991. Partitioning and purification of thaumatin in aqueous two-phase systems. Enzyme Microb Technol 13:629-635.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 629-635
    • Cascone, O.1    Andrews, B.A.2    Asenjo, J.A.3
  • 9
    • 0024962537 scopus 로고
    • Fundamental studies of biomolecule partitioning in aqueous two-phase systems
    • Diamond AD, Hsu JT. 1989. Fundamental studies of biomolecule partitioning in aqueous two-phase systems. Biotechnol Bioeng 34: 1000-1014.
    • (1989) Biotechnol Bioeng , vol.34 , pp. 1000-1014
    • Diamond, A.D.1    Hsu, J.T.2
  • 11
    • 0026281150 scopus 로고
    • A model for the prediction of partition coefficients in aqueous two-phase systems
    • Eiteman MA, Gainer JL. 1991. A model for the prediction of partition coefficients in aqueous two-phase systems. Bioseparation 2:31-41.
    • (1991) Bioseparation , vol.2 , pp. 31-41
    • Eiteman, M.A.1    Gainer, J.L.2
  • 12
    • 0030569905 scopus 로고    scopus 로고
    • Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: Effect of surface hydrophobicity
    • Franco TT, Andrews AT, Asenjo JA. 1996a. Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: effect of surface hydrophobicity. Biotechnol Bioeng 49:300-308.
    • (1996) Biotechnol Bioeng , vol.49 , pp. 300-308
    • Franco, T.T.1    Andrews, A.T.2    Asenjo, J.A.3
  • 13
    • 0030569903 scopus 로고    scopus 로고
    • Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: Effect of surface charge
    • Franco TT, Andrews AT, Asenjo JA. 1996b. Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: effect of surface charge. Biotechnol Bioeng 49:309-315.
    • (1996) Biotechnol Bioeng , vol.49 , pp. 309-315
    • Franco, T.T.1    Andrews, A.T.2    Asenjo, J.A.3
  • 14
    • 0009463974 scopus 로고
    • Precipitation
    • Asenjo JA, editor. New York: Marcel Dekker
    • Glatz CE. 1990. Precipitation. In: Asenjo JA, editor. Separation processes in biotechnology. New York: Marcel Dekker. p 329-356.
    • (1990) Separation Processes in Biotechnology , pp. 329-356
    • Glatz, C.E.1
  • 16
    • 0030589173 scopus 로고    scopus 로고
    • Hydrophobic partitioning of proteins in aqueous two-phase systems
    • Hachem FM, Andrews BA, Asenjo JA. 1996. Hydrophobic partitioning of proteins in aqueous two-phase systems. Enzyme Microb Technol 19: 507-517.
    • (1996) Enzyme Microb Technol , vol.19 , pp. 507-517
    • Hachem, F.M.1    Andrews, B.A.2    Asenjo, J.A.3
  • 17
    • 0020555760 scopus 로고
    • Use of electrophoretic titration curves for predicting optimal chromatographic conditions for fast ion-exchange chromatography of proteins
    • Haff LA, Fagerstam LG, Barry AR. 1983. Use of electrophoretic titration curves for predicting optimal chromatographic conditions for fast ion-exchange chromatography of proteins. J Chromatogr 266: 409-425.
    • (1983) J Chromatogr , vol.266 , pp. 409-425
    • Haff, L.A.1    Fagerstam, L.G.2    Barry, A.R.3
  • 18
    • 0026245037 scopus 로고
    • Purification and aqueous two-phase partitioning properties of recombinant vitreoscilla hemoglobin
    • Hart RA, Bailey JE. 1991. Purification and aqueous two-phase partitioning properties of recombinant vitreoscilla hemoglobin. Enzyme Microb Technol 13:788-795.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 788-795
    • Hart, R.A.1    Bailey, J.E.2
  • 19
    • 0016362757 scopus 로고
    • Effects of salts on the partition of proteins in aqueous polymeric biphasic systems
    • Johansson G. 1974. Effects of salts on the partition of proteins in aqueous polymeric biphasic systems. Acta Chem Scand B28:873-882.
    • (1974) Acta Chem Scand B , vol.28 , pp. 873-882
    • Johansson, G.1
  • 20
    • 0024101703 scopus 로고
    • Molecular thermodynamics of aqueous two-phase systems for bioseparation
    • King RS, Blanch HW, Prausnitz JM. 1988. Molecular thermodynamics of aqueous two-phase systems for bioseparation. AICHE J 34:1585-1594.
    • (1988) AICHE J , vol.34 , pp. 1585-1594
    • King, R.S.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 21
    • 84945277353 scopus 로고
    • Effect of salt addition on the hydrophobicities of the system and proteins in aqueous two-phase extraction systems
    • Kuboi R, Tanaka H, Komasawa I. 1991a. Effect of salt addition on the hydrophobicities of the system and proteins in aqueous two-phase extraction systems. Kagaku Kogaku Ronbunshu 17:67-74.
    • (1991) Kagaku Kogaku Ronbunshu , vol.17 , pp. 67-74
    • Kuboi, R.1    Tanaka, H.2    Komasawa, I.3
  • 22
    • 84945243935 scopus 로고
    • Separation of proteins by hydrophobic, salt and/or electrostatic effect in a aqueous two-phase extraction system
    • Kuboi R, Tanaka H, Komasawa I. 1991b. Separation of proteins by hydrophobic, salt and/or electrostatic effect in a aqueous two-phase extraction system. Kagaku Kogaku Ronbunshu 17:75-80.
    • (1991) Kagaku Kogaku Ronbunshu , vol.17 , pp. 75-80
    • Kuboi, R.1    Tanaka, H.2    Komasawa, I.3
  • 24
    • 0025527817 scopus 로고
    • Trends and future prospects of aqueous two-phase extraction
    • Kula MR. 1990. Trends and future prospects of aqueous two-phase extraction. Bioseparation 1:181-189.
    • (1990) Bioseparation , vol.1 , pp. 181-189
    • Kula, M.R.1
  • 25
    • 0022333124 scopus 로고
    • Structural interpretation of hydrodynamic measurements of proteins in solution through correlations with X-ray data
    • Kumosinski TF, Pessen H. 1985. Structural interpretation of hydrodynamic measurements of proteins in solution through correlations with X-ray data. Methods Enzymol 117:154-182.
    • (1985) Methods Enzymol , vol.117 , pp. 154-182
    • Kumosinski, T.F.1    Pessen, H.2
  • 26
    • 0028454930 scopus 로고
    • Genetically engineered charge modifications to enhance protein separation in aqueous two-phase systems: Electrochemical partitioning
    • Luther JR, Glatz CE. 1994. Genetically engineered charge modifications to enhance protein separation in aqueous two-phase systems: electrochemical partitioning. Biotechnol Bioeng 44:147-153.
    • (1994) Biotechnol Bioeng , vol.44 , pp. 147-153
    • Luther, J.R.1    Glatz, C.E.2
  • 27
    • 0018171749 scopus 로고
    • Isoelectric points of proteins: A table
    • Malamud D, Drysdale JW. 1978. Isoelectric points of proteins: a table. Anal Biochem 86:620-647.
    • (1978) Anal Biochem , vol.86 , pp. 620-647
    • Malamud, D.1    Drysdale, J.W.2
  • 28
    • 0017623134 scopus 로고
    • Salt effects on hydrophobic interactions in precipitation and chromatography of proteins; an interpretation of the lyotropic series
    • Melander W, Horváth C. 1977. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins; an interpretation of the lyotropic series. Arch Biochem Biophys 183:200-215.
    • (1977) Arch Biochem Biophys , vol.183 , pp. 200-215
    • Melander, W.1    Horváth, C.2
  • 29
    • 0030590140 scopus 로고    scopus 로고
    • Mathematical modelling and computer simulation of aqueous two-phase continuous protein extraction
    • Mistry SL, Kaul A, Merchuk JC, Asenjo JA. 1996. Mathematical modelling and computer simulation of aqueous two-phase continuous protein extraction. J Chromatogr A 741:151-163.
    • (1996) J Chromatogr A , vol.741 , pp. 151-163
    • Mistry, S.L.1    Kaul, A.2    Merchuk, J.C.3    Asenjo, J.A.4
  • 30
    • 0024662743 scopus 로고
    • Solubility-activity relationships in the inorganic salt-induced precipitation of α-chymotrypsin
    • Przybycien TM, Bailey JE. 1989. Solubility-activity relationships in the inorganic salt-induced precipitation of α-chymotrypsin. Enzyme Microb Technol 11:264-276.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 264-276
    • Przybycien, T.M.1    Bailey, J.E.2
  • 31
    • 0017312637 scopus 로고
    • Isoelectric points and molecular weights of proteins (a table)
    • Righetti PG, Caravaggio T. 1976. Isoelectric points and molecular weights of proteins (a table). J Chromatogr 127:1-28.
    • (1976) J Chromatogr , vol.127 , pp. 1-28
    • Righetti, P.G.1    Caravaggio, T.2
  • 33
    • 0028177532 scopus 로고
    • Partitioning and purification of α-amylase in aqueous two-phase systems
    • Schmidt AS, Ventom AM, Asenjo JA. 1994. Partitioning and purification of α-amylase in aqueous two-phase systems. Enzyme Microb Technol 16:131-142.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 131-142
    • Schmidt, A.S.1    Ventom, A.M.2    Asenjo, J.A.3
  • 34
    • 15844415079 scopus 로고    scopus 로고
    • Correlations for the partition behavior of proteins in aqueous two-phase systems: Effect of overall protein concentration
    • Schmidt AS, Andrews BA, Asenjo JA. 1996. Correlations for the partition behavior of proteins in aqueous two-phase systems: effect of overall protein concentration. Biotechnol Bioeng 50:617-626.
    • (1996) Biotechnol Bioeng , vol.50 , pp. 617-626
    • Schmidt, A.S.1    Andrews, B.A.2    Asenjo, J.A.3
  • 36
    • 0025143773 scopus 로고
    • Extraction of proteins from biological raw material using aqueous polyethylene glycol-citrate phase systems
    • Vernau J, Kula MR. 1990. Extraction of proteins from biological raw material using aqueous polyethylene glycol-citrate phase systems. Biotechnol Appl Biochem 12:397-404.
    • (1990) Biotechnol Appl Biochem , vol.12 , pp. 397-404
    • Vernau, J.1    Kula, M.R.2
  • 37
    • 0028283397 scopus 로고
    • Selection of chromatographic protein purification operations based on physicochemical properties
    • Watanabe E, Tsoka S, Asenjo JA. 1994. Selection of chromatographic protein purification operations based on physicochemical properties. Ann N Y Acad Sci 721:348-365.
    • (1994) Ann N Y Acad Sci , vol.721 , pp. 348-365
    • Watanabe, E.1    Tsoka, S.2    Asenjo, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.