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Volumn 100, Issue 5, 2008, Pages 941-949

Impact of clarification strategy on chromatographic separations: Pre-processing of cell homogenates

Author keywords

Centrifugation; Chromatography; Clarification; Filtration; Fouling; Hydrophobic interaction; Lipids

Indexed keywords

AGGLOMERATION; CENTRIFUGATION; CENTRIFUGES; CHROMATOGRAPHIC ANALYSIS; CHROMATOGRAPHY; CLARIFICATION; CLARIFIERS; COLUMNS (STRUCTURAL); HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; LIPIDS; LIQUID CHROMATOGRAPHY; ORGANIC COMPOUNDS; ORGANIC SOLVENTS; POROUS MATERIALS; SEPARATION; SUSPENSIONS (COMPONENTS);

EID: 48449088099     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21823     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0025700865 scopus 로고
    • The separation of affinity flocculated yeast cell debris using a pilot-plant scroll decanter centrifuge
    • Bentham AC, Bonnerjea J, Orsborn CB, Ward PN, Hoare M. 1990. The separation of affinity flocculated yeast cell debris using a pilot-plant scroll decanter centrifuge. Biotechnol Bioeng 36:397-401.
    • (1990) Biotechnol Bioeng , vol.36 , pp. 397-401
    • Bentham, A.C.1    Bonnerjea, J.2    Orsborn, C.B.3    Ward, P.N.4    Hoare, M.5
  • 2
    • 0000326098 scopus 로고
    • Reagents for enzymatic analysis: Alcohol dehydrogenase from yeast
    • Ed. 3. Weinheim: Verlag Chemie. p
    • Bermeyer HU. 1983. Reagents for enzymatic analysis: Alcohol dehydrogenase from yeast. Methods of enzymatic analysis. Ed. 3. Weinheim: Verlag Chemie. p 139-141.
    • (1983) Methods of enzymatic analysis , pp. 139-141
    • Bermeyer, H.U.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford MM. 1979. A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1979) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0029394832 scopus 로고
    • Development of an expanded bed technique for an affinity purification of G6PDH from unclarified yeast cell homogenates
    • Chang YK, McCreath GE, Chase HA. 1995. Development of an expanded bed technique for an affinity purification of G6PDH from unclarified yeast cell homogenates. Biotechnol Bioeng 48:355-366.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 355-366
    • Chang, Y.K.1    McCreath, G.E.2    Chase, H.A.3
  • 7
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum G, Lees ND, Bard M, Dickson R. 1998. Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14:1471-1496.
    • (1998) Yeast , vol.14 , pp. 1471-1496
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickson, R.4
  • 8
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross TU. 2004. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 22:1409-1414.
    • (2004) Nat Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 9
    • 84985653114 scopus 로고
    • The clarification of mechanically disrupted yeast suspensions by rotary vacuum precoat riltration
    • Gray PP, Dunnill P, Lilly MD. 1973. The clarification of mechanically disrupted yeast suspensions by rotary vacuum precoat riltration. Biotechnol Bioeng 15:309-320.
    • (1973) Biotechnol Bioeng , vol.15 , pp. 309-320
    • Gray, P.P.1    Dunnill, P.2    Lilly, M.D.3
  • 10
    • 0026059521 scopus 로고
    • Influence of system and molecular parameters upon fractionation of intracellular proteins from Saccharomyces by aqueous two-phase partition
    • Huddleston JG, Ottomar KW, Ngonyani DM, Lyddiatt A. 1991. Influence of system and molecular parameters upon fractionation of intracellular proteins from Saccharomyces by aqueous two-phase partition. Enzyme Microb Technol 13:24-32.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 24-32
    • Huddleston, J.G.1    Ottomar, K.W.2    Ngonyani, D.M.3    Lyddiatt, A.4
  • 11
    • 33749364369 scopus 로고    scopus 로고
    • Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification
    • Hutchinson N, Bingham N, Murrell N, Farid S, Hoare M. 2006. Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification. Biotechnol Bioeng 95:483-491.
    • (2006) Biotechnol Bioeng , vol.95 , pp. 483-491
    • Hutchinson, N.1    Bingham, N.2    Murrell, N.3    Farid, S.4    Hoare, M.5
  • 12
    • 33645387937 scopus 로고    scopus 로고
    • An automated microscale technique for the quantitative and parallel analysis of microfiltration operations
    • Jackson NB, Liddell JM, Lye GJ. 2006. An automated microscale technique for the quantitative and parallel analysis of microfiltration operations. J Membr Sci 276:31-41.
    • (2006) J Membr Sci , vol.276 , pp. 31-41
    • Jackson, N.B.1    Liddell, J.M.2    Lye, G.J.3
  • 13
    • 0022431056 scopus 로고
    • Column lifetime of a new agarose medium for HPLC gel filtration chromatography at basic pH
    • Johansson BL, Ellstrom C. 1985. Column lifetime of a new agarose medium for HPLC gel filtration chromatography at basic pH. J Chromatogr 330:360-364.
    • (1985) J Chromatogr , vol.330 , pp. 360-364
    • Johansson, B.L.1    Ellstrom, C.2
  • 15
    • 0031454528 scopus 로고    scopus 로고
    • An enhancement of critical flux in cross-flow microfiltration with a pretreatment of floating medium flocculator/prefilter
    • Kwon DY, Vigneswaran S, Ngo HH, Shin HS. 1997. An enhancement of critical flux in cross-flow microfiltration with a pretreatment of floating medium flocculator/prefilter. Water Sci Technol 36:267-274.
    • (1997) Water Sci Technol , vol.36 , pp. 267-274
    • Kwon, D.Y.1    Vigneswaran, S.2    Ngo, H.H.3    Shin, H.S.4
  • 16
    • 0031938841 scopus 로고    scopus 로고
    • The performance of a scaled down industrial disc stack centrifuge with a reduced feed material requirement
    • Maybury JP, Mannweiler K, Titchener-Hooker NJ, Hoare M, Dunnill P. 1998. The performance of a scaled down industrial disc stack centrifuge with a reduced feed material requirement. Bioprocess Biosyst Eng 18:191-199.
    • (1998) Bioprocess Biosyst Eng , vol.18 , pp. 191-199
    • Maybury, J.P.1    Mannweiler, K.2    Titchener-Hooker, N.J.3    Hoare, M.4    Dunnill, P.5
  • 17
    • 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
  • 19
    • 0025457152 scopus 로고
    • Selective flocculation of nucleic acids, lipids, and colloidal particles from a yeast cell homogenate by polyethyleneimine, and its scale-up
    • Milburn P, Bonnerjea J, Hoare M, Dunnill P. 1990. Selective flocculation of nucleic acids, lipids, and colloidal particles from a yeast cell homogenate by polyethyleneimine, and its scale-up. Enzyme Microb Technol 12:527-532.
    • (1990) Enzyme Microb Technol , vol.12 , pp. 527-532
    • Milburn, P.1    Bonnerjea, J.2    Hoare, M.3    Dunnill, P.4
  • 20
    • 0032868745 scopus 로고    scopus 로고
    • Purification of plasmid DNA using selective precipitation by compaction agents - A scaleable method for the liquid-phase separation of plasmid DNA from RNA
    • Murphy JC, Wibbenmeyer JA, Fox GE, Willson RC. 1999. Purification of plasmid DNA using selective precipitation by compaction agents - A scaleable method for the liquid-phase separation of plasmid DNA from RNA. Nat Biotechnol 17:822-823.
    • (1999) Nat Biotechnol , vol.17 , pp. 822-823
    • Murphy, J.C.1    Wibbenmeyer, J.A.2    Fox, G.E.3    Willson, R.C.4
  • 21
    • 0038373001 scopus 로고    scopus 로고
    • Scale-down of continuous filtration for rapid bioprocess design: Recovery and dewatering of protein precipitate suspensions
    • Reynolds T, Boychyn M, Sanderson T, Bulmer M, More J, Hoare M. 2003. Scale-down of continuous filtration for rapid bioprocess design: Recovery and dewatering of protein precipitate suspensions. Biotechnol Bioeng 83:454-464.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 454-464
    • Reynolds, T.1    Boychyn, M.2    Sanderson, T.3    Bulmer, M.4    More, J.5    Hoare, M.6
  • 23
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter R, Brügger B, Sandhoff R, Zellnig G, Leber A, Lampl M, Athenstaedt K, Hrastnik C, Eder S, Daum G, Paltauf F, Wieland FT, Kohlwein SD. 1999. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J Cell Biol 146:741-754.
    • (1999) J Cell Biol , vol.146 , pp. 741-754
    • Schneiter, R.1    Brügger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12    Kohlwein, S.D.13
  • 25
    • 33745943608 scopus 로고    scopus 로고
    • Effect of fouling on the capacity and breakthrough characteristics of a packed bed ion exchange chromatography column
    • Siu SC, Baldascini H, Hearle DC, Hoare M, Titchener-Hooker NJ. 2006b Effect of fouling on the capacity and breakthrough characteristics of a packed bed ion exchange chromatography column. Bioprocess Biosyst Eng 28:405-414.
    • (2006) Bioprocess Biosyst Eng , vol.28 , pp. 405-414
    • Siu, S.C.1    Baldascini, H.2    Hearle, D.C.3    Hoare, M.4    Titchener-Hooker, N.J.5
  • 27
    • 0037199638 scopus 로고    scopus 로고
    • Hydrophobic interaction ligand selection and scale-up of an expanded bed separation of an intracellular enzyme from Saccharomyces cerevisiae
    • Smith MP, Bulmer MA, Hjorth R, Titchener-Hooker NJ. 2002. Hydrophobic interaction ligand selection and scale-up of an expanded bed separation of an intracellular enzyme from Saccharomyces cerevisiae. J Chromatogr A 968:121-128.
    • (2002) J Chromatogr A , vol.968 , pp. 121-128
    • Smith, M.P.1    Bulmer, M.A.2    Hjorth, R.3    Titchener-Hooker, N.J.4
  • 29
    • 0035174933 scopus 로고    scopus 로고
    • Quantification of plasma membrane ergosterol of Saccharomyces cervisiae by direct-injection atmospheric pressure chemical ionization/tandem mass spectrometry
    • Toh TH, Prior BA, van der Merwe MJ. 2001. Quantification of plasma membrane ergosterol of Saccharomyces cervisiae by direct-injection atmospheric pressure chemical ionization/tandem mass spectrometry. Anal Biochem 288:44-51.
    • (2001) Anal Biochem , vol.288 , pp. 44-51
    • Toh, T.H.1    Prior, B.A.2    van der Merwe, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.