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Volumn 62, Issue 3, 1999, Pages 247-258

Protein purification with vapor-phase carbon dioxide

Author keywords

CO2; Fractional precipitation; GAS; Gaseous antisolvent; Proteins

Indexed keywords

BIOASSAY; CARBON DIOXIDE; ELECTROPHORESIS; ENZYMES; INSULIN; MIXTURES; PHOSPHORUS COMPOUNDS; PRECIPITATION (CHEMICAL); PURIFICATION; SEPARATION; SOLUBILITY; SULFUR COMPOUNDS;

EID: 0033524721     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19990205)62:3<247::AID-BIT1>3.0.CO;2-S     Document Type: Article
Times cited : (47)

References (56)
  • 1
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. 1996. How Hofmeister ion interactions affect protein stability. Biophysical J 71:2056-2063.
    • (1996) Biophysical J , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 2
    • 0030072124 scopus 로고    scopus 로고
    • Crystallization of phenanthrene from toluene with carbon dioxide by the GAS process
    • Berends EM, Bruinsma OSL, de Graauw J, van Rosmalen GM. 1996. Crystallization of phenanthrene from toluene with carbon dioxide by the GAS process. AIChE J 42:431-439.
    • (1996) AIChE J , vol.42 , pp. 431-439
    • Berends, E.M.1    Bruinsma, O.S.L.2    De Graauw, J.3    Van Rosmalen, G.M.4
  • 4
    • 0023933377 scopus 로고
    • Structure of the bovine pancreatic ribonuclease gene-the unique intervening sequence in the 5′ untranslated region contains a promoter-like element
    • Carsana A, Confalone E, Palmieri M, Libonati M, Furia A. 1988. Structure of the bovine pancreatic ribonuclease gene-the unique intervening sequence in the 5′ untranslated region contains a promoter-like element. Nucleic Acids Res 16:5491-5502.
    • (1988) Nucleic Acids Res , vol.16 , pp. 5491-5502
    • Carsana, A.1    Confalone, E.2    Palmieri, M.3    Libonati, M.4    Furia, A.5
  • 5
    • 0022677689 scopus 로고
    • The kinetics of protein precipitation by different reagents
    • Chan MYY, Hoare M, Dunnill P. 1986. The kinetics of protein precipitation by different reagents. Biotechnol Bioeng 28:387-393.
    • (1986) Biotechnol Bioeng , vol.28 , pp. 387-393
    • Chan, M.Y.Y.1    Hoare, M.2    Dunnill, P.3
  • 6
    • 0025861876 scopus 로고
    • Protein separation and purification in neat dimethyl-sulfoxide
    • Chang N, Hen SJ, Klibanov AM. 1991. Protein separation and purification in neat dimethyl-sulfoxide. Biochem Biophys Res Comm 176:1462-1468.
    • (1991) Biochem Biophys Res Comm , vol.176 , pp. 1462-1468
    • Chang, N.1    Hen, S.J.2    Klibanov, A.M.3
  • 7
    • 0000578362 scopus 로고
    • The mechanism of floc formation in protein precipitation by polyelectrolytes
    • Chen W, Walker S, Berg JC. 1992. The mechanism of floc formation in protein precipitation by polyelectrolytes. Chem Eng Sci 47:1039-1045.
    • (1992) Chem Eng Sci , vol.47 , pp. 1039-1045
    • Chen, W.1    Walker, S.2    Berg, J.C.3
  • 8
    • 0027596095 scopus 로고
    • The effect of polyelectrolyte dosage on floc formation in protein precipitation by polyelectrolytes
    • Chen W, Berg JC. 1993. The effect of polyelectrolyte dosage on floc formation in protein precipitation by polyelectrolytes. Chem Eng Sci 48:1775-1784.
    • (1993) Chem Eng Sci , vol.48 , pp. 1775-1784
    • Chen, W.1    Berg, J.C.2
  • 10
    • 0023561734 scopus 로고
    • Polymer dosage considerations in polyelectrolyte precipitation of proteins
    • Clark KM, Glatz CE. 1987. Polymer dosage considerations in polyelectrolyte precipitation of proteins. Biotechnol Prog 3:241-247.
    • (1987) Biotechnol Prog , vol.3 , pp. 241-247
    • Clark, K.M.1    Glatz, C.E.2
  • 11
    • 0027273987 scopus 로고
    • Aggregation and denaturation of apomyoglobin in aqueous urea solutions
    • DeYoung LR, Dill KA, Fink AL. 1993. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochem 32:3877-3886.
    • (1993) Biochem , vol.32 , pp. 3877-3886
    • DeYoung, L.R.1    Dill, K.A.2    Fink, A.L.3
  • 12
    • 0026239830 scopus 로고
    • Molecular thermodynamics of solubilities in GAS crystallization
    • Dixon DJ, Johnston KP. 1991. Molecular thermodynamics of solubilities in GAS crystallization. AIChE J 37:1441-1449.
    • (1991) AIChE J , vol.37 , pp. 1441-1449
    • Dixon, D.J.1    Johnston, K.P.2
  • 13
    • 0027791058 scopus 로고
    • Formation of microporous polymer fibers and oriented fibrils by precipitation with a compressed fluid antisolvent
    • Dixon DJ, Johnston KP. 1993. Formation of microporous polymer fibers and oriented fibrils by precipitation with a compressed fluid antisolvent. J Appl Polym Sci 50:1929-1942.
    • (1993) J Appl Polym Sci , vol.50 , pp. 1929-1942
    • Dixon, D.J.1    Johnston, K.P.2
  • 14
    • 0027333734 scopus 로고
    • Polymeric materials formed by precipitation with a compressed fluid antisolvent
    • Dixon DJ, Johnston KP, Bodmeir RA. 1993. Polymeric materials formed by precipitation with a compressed fluid antisolvent. AIChE J 39:127-139.
    • (1993) AIChE J , vol.39 , pp. 127-139
    • Dixon, D.J.1    Johnston, K.P.2    Bodmeir, R.A.3
  • 15
    • 0021697311 scopus 로고
    • Scaling up bio-product separations with high performance liquid chromatography
    • Dwyer JL. 1984. Scaling up bio-product separations with high performance liquid chromatography. Bio/Technol 2:957-964.
    • (1984) Bio/Technol , vol.2 , pp. 957-964
    • Dwyer, J.L.1
  • 16
    • 0029659151 scopus 로고    scopus 로고
    • Supercritical fluids as solvents for chemical and materials processing
    • Eckert CA, Knutson BL, Debenedetti PG. 1996. Supercritical fluids as solvents for chemical and materials processing. Nature 383:313-318.
    • (1996) Nature , vol.383 , pp. 313-318
    • Eckert, C.A.1    Knutson, B.L.2    Debenedetti, P.G.3
  • 17
    • 0025209804 scopus 로고
    • Precipitation techniques
    • Englard S, Seifer S. 1990. Precipitation techniques. Meth Enzymol 182: 285-300.
    • (1990) Meth Enzymol , vol.182 , pp. 285-300
    • Englard, S.1    Seifer, S.2
  • 18
    • 0022752656 scopus 로고
    • Effects of mixing during acid addition on fractionally precipitated protein
    • Fisher RR, Glatz CE, Murphy PA. 1986. Effects of mixing during acid addition on fractionally precipitated protein. Biotechnol Bioeng 28:1056-1063.
    • (1986) Biotechnol Bioeng , vol.28 , pp. 1056-1063
    • Fisher, R.R.1    Glatz, C.E.2    Murphy, P.A.3
  • 19
    • 0000746640 scopus 로고
    • Gas antisolvent recrystallization: New process to recrystallize compounds insoluble in supercritical fluids
    • Johnston KP and Penninger JML, editors. Supercritical fluid science and technology. American Chemical Society, Washington, D.C.
    • Gallagher PM, Coffey MP, Krukonis VJ, Klasutis N. 1989. Gas antisolvent recrystallization: New process to recrystallize compounds insoluble in supercritical fluids. In: Johnston KP and Penninger JML, editors. Supercritical fluid science and technology. ACS Symp. Ser. 406. American Chemical Society, Washington, D.C. p 334-354.
    • (1989) ACS Symp. Ser. 406 , vol.406 , pp. 334-354
    • Gallagher, P.M.1    Coffey, M.P.2    Krukonis, V.J.3    Klasutis, N.4
  • 20
    • 0000712830 scopus 로고
    • Gas anti-solvent recrystallization of RDX: Formation of ultra-fine particles of a difficult-to-comminute explosive
    • Gallagher PM, Coffey MP, Krukonis VJ. 1992. Gas anti-solvent recrystallization of RDX: Formation of ultra-fine particles of a difficult-to-comminute explosive. J Supercritical Fluids 5:130-142.
    • (1992) J Supercritical Fluids , vol.5 , pp. 130-142
    • Gallagher, P.M.1    Coffey, M.P.2    Krukonis, V.J.3
  • 21
    • 0025843479 scopus 로고
    • A kinetic study of the compelition between renaturation and aggregation during the refolding of denatured reduced egg-white lysozyme
    • Goldberg ME, Rudolph R, Jaenicke R. 1991. A kinetic study of the compelition between renaturation and aggregation during the refolding of denatured reduced egg-white lysozyme. Biochem 30:2790-2797.
    • (1991) Biochem , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 22
    • 0026620720 scopus 로고
    • Conformational changes in cubic insulin crystals
    • Gursky O, Badger J, Li Y, Caspar DLD. 1992. Conformational changes in cubic insulin crystals. J Biophys 63:1210-1220.
    • (1992) J Biophys , vol.63 , pp. 1210-1220
    • Gursky, O.1    Badger, J.2    Li, Y.3    Caspar, D.L.D.4
  • 23
    • 0020971013 scopus 로고
    • Reactor design for protein precipitation and its effect on centrifugal separation
    • Hoare M, Dunnill P, Bell DJ. 1983. Reactor design for protein precipitation and its effect on centrifugal separation. Ann NY Acad Sci 413:254-269.
    • (1983) Ann NY Acad Sci , vol.413 , pp. 254-269
    • Hoare, M.1    Dunnill, P.2    Bell, D.J.3
  • 24
    • 0025261698 scopus 로고
    • Protein precipitation with polyethylene glycol
    • Ingham KC. 1990. Protein precipitation with polyethylene glycol. Meth Enzymol 182:301-306.
    • (1990) Meth Enzymol , vol.182 , pp. 301-306
    • Ingham, K.C.1
  • 25
    • 0028372337 scopus 로고
    • Protein precipitation: Effects of mixing on protein solubility
    • Iyer HV, Przybycien TM. 1994. Protein precipitation: Effects of mixing on protein solubility. AIChE J 40:349-360.
    • (1994) AIChE J , vol.40 , pp. 349-360
    • Iyer, H.V.1    Przybycien, T.M.2
  • 26
    • 0029637138 scopus 로고
    • Multipoint binding and heterogeneity in immobilized metal affinity-chromatography
    • Johnson RD, Arnold FH. 1995. Multipoint binding and heterogeneity in immobilized metal affinity-chromatography. Biotechnol Bioeng 48:437-443.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 437-443
    • Johnson, R.D.1    Arnold, F.H.2
  • 27
    • 0001000486 scopus 로고
    • Lysozymes from rabbit spleen and dog spleen
    • Jollés P. 1962. Lysozymes from rabbit spleen and dog spleen. Meth Enzymol 5:137-146.
    • (1962) Meth Enzymol , vol.5 , pp. 137-146
    • Jollés, P.1
  • 28
    • 0019143031 scopus 로고
    • Exons encode functional and structural units of chicken lysozyme
    • Jung A, Sippel AE, Grez M, Schutz G. 1980. Exons encode functional and structural units of chicken lysozyme. Proc Natl Acad Sci USA 77:5759-5763.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5759-5763
    • Jung, A.1    Sippel, A.E.2    Grez, M.3    Schutz, G.4
  • 29
    • 58149325322 scopus 로고
    • Volume expansions and vapor-liquid equilibria of binary mixtures of a variety of polar solvents and certain near-critical solvents
    • Kordikowski A, Schenk AP, Van Nielen RM, Peters CJ. 1995. Volume expansions and vapor-liquid equilibria of binary mixtures of a variety of polar solvents and certain near-critical solvents. J Supercritical Fluids 8:205-216.
    • (1995) J Supercritical Fluids , vol.8 , pp. 205-216
    • Kordikowski, A.1    Schenk, A.P.2    Van Nielen, R.M.3    Peters, C.J.4
  • 30
    • 84872631302 scopus 로고
    • A spectrophotometric method for the measurement of ribonuclease activity
    • Kunitz M. 1946. A spectrophotometric method for the measurement of ribonuclease activity. J Biol Chem 164:563-568.
    • (1946) J Biol Chem , vol.164 , pp. 563-568
    • Kunitz, M.1
  • 31
    • 0025009050 scopus 로고
    • Isolation and nucleotide-sequence of CDNA clone for bovine pancreatic anionic trypsinogen-Structural identity with the trypsin family
    • Le Huerou I, Wicker C, Guilloteau P, Toullec R, Puigserver A. 1990. Isolation and nucleotide-sequence of CDNA clone for bovine pancreatic anionic trypsinogen-Structural identity with the trypsin family. Eur J Biochem 193:767-773.
    • (1990) Eur J Biochem , vol.193 , pp. 767-773
    • Huerou L. I1    Wicker, C.2    Guilloteau, P.3    Toullec, R.4    Puigserver, A.5
  • 32
    • 0029666602 scopus 로고    scopus 로고
    • Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte
    • Li YJ, Mattison KW, Dubin PL, Havel HA, Edwards SL. 1996. Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte. Biopolymers 38:527-533.
    • (1996) Biopolymers , vol.38 , pp. 527-533
    • Li, Y.J.1    Mattison, K.W.2    Dubin, P.L.3    Havel, H.A.4    Edwards, S.L.5
  • 33
    • 0029347292 scopus 로고
    • Semi-crystalline microfibrils and hollow fibres by precipitation with a compressed-fluid antisolvent
    • Luna-Bárcenas G, Kanakia SK, Sanchez IC, Johnston KP. 1995. Semi-crystalline microfibrils and hollow fibres by precipitation with a compressed-fluid antisolvent. Polymers 36:3173-3182.
    • (1995) Polymers , vol.36 , pp. 3173-3182
    • Luna-Bárcenas, G.1    Kanakia, S.K.2    Sanchez, I.C.3    Johnston, K.P.4
  • 34
    • 0020971010 scopus 로고
    • Large-scale isolation and purification of proteins from recombinant E. Coli
    • McGregor WC. 1983. Large-scale isolation and purification of proteins from recombinant E. coli. Ann NY Acad Sci 413:231-237.
    • (1983) Ann NY Acad Sci , vol.413 , pp. 231-237
    • McGregor, W.C.1
  • 35
    • 0001706952 scopus 로고
    • Separating polymer-solutions with supercritical fluids
    • McHugh MA, Guckes TL. 1985. Separating polymer-solutions with supercritical fluids. Macromolecules 18:674-680.
    • (1985) Macromolecules , vol.18 , pp. 674-680
    • McHugh, M.A.1    Guckes, T.L.2
  • 36
    • 0023186584 scopus 로고
    • Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis
    • Nakayama A, Kawamura K, Shimada H, Akaoka A, Mita I, Honjo M, Furutani Y. 1987. Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis. J Biotechnol 5:171-179.
    • (1987) J Biotechnol , vol.5 , pp. 171-179
    • Nakayama, A.1    Kawamura, K.2    Shimada, H.3    Akaoka, A.4    Mita, I.5    Honjo, M.6    Furutani, Y.7
  • 37
    • 0022144820 scopus 로고
    • Primary particle formation in protein precipitation
    • Nelson CD, Glatz CE 1985. Primary particle formation in protein precipitation. Biotechnol Bioeng 27:1434-1444.
    • (1985) Biotechnol Bioeng , vol.27 , pp. 1434-1444
    • Nelson, C.D.1    Glatz, C.E.2
  • 39
    • 0001915139 scopus 로고
    • Challenges for chemical engineers in the pharmaceulical industry
    • Paul EL, Rosas CB. 1990. Challenges for chemical engineers in the pharmaceulical industry. Chem Eng Prog 22:17-25.
    • (1990) Chem Eng Prog , vol.22 , pp. 17-25
    • Paul, E.L.1    Rosas, C.B.2
  • 40
    • 0023006886 scopus 로고
    • Affinity precipitation of lactate-dehydrogenase with triazine dye derivative-selective precipitation of rabbit muscle lactate-dehydrogenase with a procion blue H-B analog
    • Pearson JC, Burton SJ, Lowe CR. 1986. Affinity precipitation of lactate-dehydrogenase with triazine dye derivative-selective precipitation of rabbit muscle lactate-dehydrogenase with a procion blue H-B analog. Analyt Biochem 158:382-389.
    • (1986) Analyt Biochem , vol.158 , pp. 382-389
    • Pearson, J.C.1    Burton, S.J.2    Lowe, C.R.3
  • 41
    • 0024713895 scopus 로고
    • Preparative affinity precipitation of L-lactate dehydrogenase
    • Pearson JC, Clonis YD, Lowe CR. 1989. Preparative affinity precipitation of L-lactate dehydrogenase. J Biotechnol 11:267-274.
    • (1989) J Biotechnol , vol.11 , pp. 267-274
    • Pearson, J.C.1    Clonis, Y.D.2    Lowe, C.R.3
  • 42
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. Which is more generally applicable
    • Peterson GL. 1977. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346-356.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 43
    • 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. Enz Microb Technol 11:264-276.
    • (1989) Enz Microb Technol , vol.11 , pp. 264-276
    • Przybycien, T.M.1    Bailey, J.E.2
  • 44
    • 0000009935 scopus 로고
    • A preliminary study of the properties of proteins in some nonaqueous solvents
    • Rees ED, Singer SJ. 1956. A preliminary study of the properties of proteins in some nonaqueous solvents. Arch Biochem Biophys 63:144-159.
    • (1956) Arch Biochem Biophys , vol.63 , pp. 144-159
    • Rees, E.D.1    Singer, S.J.2
  • 46
    • 0023828997 scopus 로고
    • High-pressure solution behavior of the polystyrene-toluene-ethane system
    • Seckner AJ, McClellan AK, McHugh MA. 1988. High-pressure solution behavior of the polystyrene-toluene-ethane system. AIChE J 34:9-16.
    • (1988) AIChE J , vol.34 , pp. 9-16
    • Seckner, A.J.1    McClellan, A.K.2    McHugh, M.A.3
  • 47
    • 0024618118 scopus 로고
    • Affinity-precipitation using chitosan as ligand carrier
    • Senstad C, Mattiasson B. 1989. Affinity-precipitation using chitosan as ligand carrier. Biotechnol Appl Bioeng 11:41-48.
    • (1989) Biotechnol Appl Bioeng , vol.11 , pp. 41-48
    • Senstad, C.1    Mattiasson, B.2
  • 48
    • 0024700283 scopus 로고
    • Purification of wheat-germ agglutinin using affinity flocculation with chitosan and a subsequent centrifugation or flotation step
    • Senstad C, Mattiasson B. 1990. Purification of wheat-germ agglutinin using affinity flocculation with chitosan and a subsequent centrifugation or flotation step. Biotechnol Bioeng 34:387-393.
    • (1990) Biotechnol Bioeng , vol.34 , pp. 387-393
    • Senstad, C.1    Mattiasson, B.2
  • 49
    • 0027113003 scopus 로고
    • Some characteristics of protein precipitation by salts
    • Shih YC, Prausnitz JM, Blanch HW. 1992. Some characteristics of protein precipitation by salts. Biotechnol Bioeng 40:1155-1164.
    • (1992) Biotechnol Bioeng , vol.40 , pp. 1155-1164
    • Shih, Y.C.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 50
    • 77956714255 scopus 로고
    • The properties of proteins in nonaqueous solvents
    • Singer SJ. 1962. The properties of proteins in nonaqueous solvents. Adv Protein Chem 17:1-68.
    • (1962) Adv Protein Chem , vol.17 , pp. 1-68
    • Singer, S.J.1
  • 51
    • 0027409286 scopus 로고
    • Cloning and expression of the bovine intestinal alkaline phosphatase gene-biochemical characterization of the recombinant enzyme
    • Weissig H, Schildge A, Hoylaerts MF, Iobal M, Millan JL. 1993. Cloning and expression of the bovine intestinal alkaline phosphatase gene-biochemical characterization of the recombinant enzyme. Biochem J 290:503-508.
    • (1993) Biochem J , vol.290 , pp. 503-508
    • Weissig, H.1    Schildge, A.2    Hoylaerts, M.F.3    Iobal, M.4    Millan, J.L.5
  • 53
    • 0027909016 scopus 로고
    • Formation of microparticulate protein powders using a supercritical fluid antisolvent
    • Yeo SD, Lim GB, Debenedetti PG, Bernstein H. 1993a. Formation of microparticulate protein powders using a supercritical fluid antisolvent. Biotechnol Bioeng 41:341-346.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 341-346
    • Yeo, S.D.1    Lim, G.B.2    Debenedetti, P.G.3    Bernstein, H.4
  • 54
    • 0027912466 scopus 로고
    • Supercritical antisolvent process for substituted para-linked aromatic polyamides: Phase equilibrium and morphology study
    • Yeo SD, Debenedetti PG, Radosz M, Schmidt HW. 1993b. Supercritical antisolvent process for substituted para-linked aromatic polyamides: Phase equilibrium and morphology study. Macromolecules 26:6207-6210.
    • (1993) Macromolecules , vol.26 , pp. 6207-6210
    • Yeo, S.D.1    Debenedetti, P.G.2    Radosz, M.3    Schmidt, H.W.4
  • 55
    • 0028597537 scopus 로고
    • Secondary structure characterization of microparticulate insulin powders
    • Yeo SD, Debenedetti PG, Patro S, Przybycien TM. 1994. Secondary structure characterization of microparticulate insulin powders. J Pharm Sci 83:1651-1656.
    • (1994) J Pharm Sci , vol.83 , pp. 1651-1656
    • Yeo, S.D.1    Debenedetti, P.G.2    Patro, S.3    Przybycien, T.M.4
  • 56
    • 0029247107 scopus 로고
    • Supercritical antisolvent process for a series of substituted para-linked aromatic polyamides
    • Yeo SD, Debenedetti PG, Radosz M, Giesa R, Schmidt HW. 1995. Supercritical antisolvent process for a series of substituted para-linked aromatic polyamides. Macromolecules 28:1316-1417.
    • (1995) Macromolecules , vol.28 , pp. 1316-1417
    • Yeo, S.D.1    Debenedetti, P.G.2    Radosz, M.3    Giesa, R.4    Schmidt, H.W.5


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