Optimization of preparative hydrophobic interaction chromatographic purification methods.
J Chromatogr
; 359: 331-7, 1986 May 30.
Article
em En
| MEDLINE
| ID: mdl-3733935
ABSTRACT
The chromatographic behavior of five proteins on hydrophobic interaction matrices having six different ligand arms was investigated using gradient elution with ammonium sulfate and ammonium acetate buffers at two pH values. The nature of the mobile phase and/or the ligand chain arm of the matrix was found to have substantial effect on the resolution, retention, and selectivity. Ovalbumin was moderately or highly retained with ammonium sulfate on all columns; however, with ammonium acetate, ovalbumin was not retained on SynChropak Hydroxypropyl and Propyl columns. Chromatographic conditions developed for analytical hydrophobic interaction chromatography columns containing 6.5-micron packings were adapted to preparative columns packed with 30-micron SynChroprep packings for the separation of serum components. Dynamic load capacities were 4-13 mg of ovalbumin per ml of column volume.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Chromatogr
Ano de publicação:
1986
Tipo de documento:
Article