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Titolo:
Selectivity of IMAC columns in trypsin inhibitor purification
Autore:
Yeomans-Reina, H; Ruiz-Manriquez, A; Wong, BR; Mansir, AT;
Indirizzi:
Univ Sonora, Dept Ingn Quim & Met, Mexico City, DF, Mexico Univ Sonora Mexico City DF Mexico gn Quim & Met, Mexico City, DF, Mexico Univ Sonora, Dept Invest Alimentos, Mexico City, DF, Mexico Univ Sonora Mexico City DF Mexico est Alimentos, Mexico City, DF, Mexico Univ Sonora, Dept Invest Cient & Tecnol, Mexico City, DF, Mexico Univ Sonora Mexico City DF Mexico ient & Tecnol, Mexico City, DF, Mexico
Titolo Testata:
BIOTECHNOLOGY PROGRESS
fascicolo: 4, volume: 17, anno: 2001,
pagine: 729 - 733
SICI:
8756-7938(200107/08)17:4<729:SOICIT>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND AFFINITY-CHROMATOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
14
Recensione:
Indirizzi per estratti:
Indirizzo: Yeomans-Reina, H Univ Sonora, Dept Ingn Quim & Met, Mexico City, DF, Mexico Univ Sonora Mexico City DF Mexico xico City, DF, Mexico
Citazione:
H. Yeomans-Reina et al., "Selectivity of IMAC columns in trypsin inhibitor purification", BIOTECH PR, 17(4), 2001, pp. 729-733

Abstract

The properties of an adsorbent and the parameters in an adsorption processaffect the resolution of chromatographic purifications. This is reflected in the elution profile, which shows the relative affinity of different proteins for a specific adsorbent. In the work presented here, elution profilesfor trypsin inhibitor were used to study the effects of the concentration of trypsin inhibitor, ionic strength of the protein solution, slope of the elution gradient, and the regeneration treatment of the chromatography column on the selectivity of the adsorbent Cellufine Chelate-Cu-II(ida). Cytochrome c was used as a reference protein. Variations in the concentrations oftrypsin inhibitor and in the ionic strength of the buffered solution did not have any effects on the elution profile. On the other hand, changes in the slope of the pH gradient used for elution caused shifting of the elutionpeaks toward lower values of the elution volume, resulting in the best strategy to modify the elution profile of the system. Finally, using a constant slope pH gradient of elution, the variation of the selectivity of the adsorbent for trypsin inhibitor when subjected to cleaning treatments with 0.5N NaOH was studied. Appropriate cleaning practices used in industry were followed. The adsorbent showed only a slight tendency for resolution loss inthe order of 2 x 10(-4) days(-1). The results presented here show a good stability of the adsorbent when compared to other biospecific adsorbents commonly used.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 19:00:09