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| Tanaka,K.; Shigueoka,E.M.; Sawatani,E.; Dias,G.A.; Arashiro,F.; Campos,T.C.X.B.; Nakao,H.C.. |
| Large volumes of plasma can be fractionated by the method of Cohn at low cost. However, liquid chromatography is superior in terms of the quality of the product obtained. In order to combine the advantages of each method, we developed an integrated method for the production of human albumin and immunoglobulin G (IgG). The cryoprecipitate was first removed from plasma for the production of factor VIII and the supernatant of the cryoprecipitate was fractionated by the method of Cohn. The first precipitate, containing fractions (F)-I + II + III, was used for the production of IgG by the chromatographic method (see Tanaka K et al. (1998) Brazilian Journal of Medical and Biological Research, 31: 1375-1381). The supernatant of F-I + II + III was submitted to a... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Albumin production; Industrial chromatography; Hemoderivate production; Downstream process; Plasma derivatives. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001100003 |
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| Tanaka,K.; Sawatani,E.; Dias,G.A.; Shigueoka,E.M.; Campos,T.C.X.B.; Nakao,H.C.; Arashiro,F.. |
| In order to obtain intravenous immunoglobulin G (iv IgG) of high quality from F-I+II+III or F-II+III pastes prepared by the Cohn method, we developed a chromatography process using ion exchange gels, Q-Sepharose FF and CM-Sepharose FF, and Sephacryl S-300 gel filtration. Viral inactivation was performed by incubating the preparation with pepsin at pH 4.0 at 35oC for 18 h. The characteristics of 28 batches produced by us were: yield 4.3 ± 0.2 g/l plasma, i.e., a recovery of 39.1 ± 1.8%; IgG subclasses distribution: IgG1 = 58.4%, IgG2 = 34.8%, IgG3 = 4.5% and IgG4 = 2.3%; IgG size distribution was 98.4% monomers, 1.2% dimers and 0.4% polymers and protein aggregates; anticomplement activity was less than 0.5 CH50/mg IgG, and prekallikrein activator activity... |
| Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Immunoglobulin G purification; Hemoderivative purification; Chromatographic procedures; High quality immunoglobulin G; Downstream process. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000100004 |
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| Tanaka,K.; Sawatani,E.; Shigueoka,E.M.; Campos,T.C.X.B.; Nakao,H.C.; Dias,G.A.; Fujita,R.K.; Arashiro,F.. |
| Immunoglobulin G (IgG) of excellent quality for intravenous use was obtained from the cryosupernatant of human plasma by a chromatographic method based on a mixture of ion-exchange, DEAE-Sepharose FF and arginine Sepharose 4B affinity chromatography and a final purification step by Sephacryl S-300 HR gel filtration. The yield of 10 experimental batches produced was 3.5 g IgG per liter of plasma. A solvent/detergent combination of 1% Tri (n-butyl) phosphate and 1% Triton X-100 was used to inactivate lipid-coated viruses. Analysis of the final product (5% liquid IgG) based on the mean for 10 batches showed 94% monomers, 5.5% dimers and 0.5% polymers and aggregates. Anticomplementary activity was 0.3 CH50/mg IgG and prekallikrein activator levels were less... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Immunoglobulin G production; Hemoderivate production; Intravenous gamma globulin production; Industrial chromatography; Downstream process. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001100002 |
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| Tanaka,K.; Sawatani,E.; Shigueoka,E.M.; Dias,G.A.; Nakao,H.C.; Arashiro,F.. |
| The aim of the method described here is to remove hemoglobin, the major contaminant in the bovine plasma obtained from slaughterhouses, by adding a mixture of 19% cold ethanol and 0.6% chloroform, followed by fibrinogen and globulin precipitation by the Cohn method and nonspecific hemagglutinin by thermocoagulation. The experimental volume of bovine plasma was 2,000 ml per batch. Final purification was performed by liquid chromatography using the ion-exchange gel DEAE-Sepharose FF. The bovine albumin thus obtained presented > or = 99% purity, a yield of 25.0 ± 1.2 g/l plasma and >71.5% recovery. N-acetyl-DL-tryptophan (0.04 mmol/g protein) and sodium caprylate (0.04 mmol/g protein) were used as stabilizers and the final concentration of albumin was... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bovine albumin; Production bovine albumin; Purification bovine albumin; Polymerization bovine albumin; Downstream process. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000800002 |
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