dc.creator | Borsoi-Ribeiro, Mariana | |
dc.creator | Bresolin, Igor Tadeu Lazzarotto | |
dc.creator | Vijayalakshmi, Mookambeswaran | |
dc.creator | Bueno, Sônia Maria Alves | |
dc.date | 2013-Oct | |
dc.date | 2015-11-27T13:32:07Z | |
dc.date | 2015-11-27T13:32:07Z | |
dc.date.accessioned | 2018-03-29T01:18:26Z | |
dc.date.available | 2018-03-29T01:18:26Z | |
dc.identifier | Journal Of Molecular Recognition : Jmr. v. 26, n. 10, p. 514-20, 2013-Oct. | |
dc.identifier | 1099-1352 | |
dc.identifier | 10.1002/jmr.2296 | |
dc.identifier | http://www.ncbi.nlm.nih.gov/pubmed/23996494 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/200801 | |
dc.identifier | 23996494 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1301034 | |
dc.description | Iminodiacetic acid (IDA) and tris(2-aminoethyl)amine (TREN) chelating ligands were immobilized on poly(ethylene vinyl alcohol) (PEVA) hollow-fiber membranes after activation with epichlorohydrin or butanediol diglycidyl ether (bisoxirane). The affinity membranes complexed with Cu(II) were evaluated for adsorption of human immunoglobulin G (IgG). The effects of matrix activation and buffer system on adsorption of IgG were studied. Isotherms of batch IgG adsorption onto finely cut membranes showed that neither of the chelates, IDA-Cu(II) or TREN-Cu(II), had a Langmuirean behavior with negative cooperativity for IgG binding. A comparison of equilibrium and dynamic maximum capacities showed that the dynamic capacity for a mini-cartridge in a cross-flow filtration mode (52.5 and 298.4 mg g(-1) dry weight for PEVA-TREN-Cu(II) and PEVA-IDA-Cu(II), respectively) was somewhat higher than the equilibrium capacity (9.2 and 73.3 mg g(-1) dry weight for PEVA-TREN-Cu(II) and PEVA-IDA-Cu(II), respectively). When mini-cartridges were used, the dynamic adsorption capacity of IDA-Cu(II) was the same for both mini-cartridge and agarose gel. | |
dc.description | 26 | |
dc.description | 514-20 | |
dc.language | eng | |
dc.relation | Journal Of Molecular Recognition : Jmr | |
dc.relation | J. Mol. Recognit. | |
dc.rights | fechado | |
dc.rights | Copyright © 2013 John Wiley & Sons, Ltd. | |
dc.source | PubMed | |
dc.subject | Adsorption | |
dc.subject | Cations, Divalent | |
dc.subject | Chelating Agents | |
dc.subject | Chromatography, Affinity | |
dc.subject | Copper | |
dc.subject | Epichlorohydrin | |
dc.subject | Epoxy Compounds | |
dc.subject | Ethylenediamines | |
dc.subject | Imino Acids | |
dc.subject | Immunoglobulin G | |
dc.subject | Kinetics | |
dc.subject | Membranes, Artificial | |
dc.subject | Polyvinyls | |
dc.subject | Protein Binding | |
dc.subject | Solutions | |
dc.subject | Thermodynamics | |
dc.subject | Cu(ii) | |
dc.subject | Imac | |
dc.subject | Adsorption | |
dc.subject | Affinity Membranes | |
dc.subject | Human Igg | |
dc.subject | Tris(2-aminoethyl)amine | |
dc.title | Behavior Of Human Immunoglobulin G Adsorption Onto Immobilized Cu(ii) Affinity Hollow-fiber Membranes. | |
dc.type | Artículos de revistas | |