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A scale‐down study into the chromatography of a peptide using the cation‐exchange cellulose, Express‐Ion C
Author(s) -
Levison Peter R,
Streater Michael,
Dennis Jon W
Publication year - 1999
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199903)74:3<204::aid-jctb30>3.0.co;2-2
Subject(s) - desorption , chemistry , chromatography , cellulose , peptide , ion exchange , ion chromatography , ion exchange resin , column chromatography , ion , adsorption , organic chemistry , biochemistry
The chromatography of the peptide His‐ D ‐Trp‐Ala‐Trp‐ D ‐Phe‐Lys‐NH 2 on the cation‐exchange cellulose Whatman Express‐Ion Exchanger C has been investigated. Scale‐down studies both in batch and using Mini Columns demonstrated a binding capacity of ∽300 mg per dry g and a recovery following desorption of ∽96%. The separation was scaled‐up 40‐fold to a laboratory column, where 100% (w/w) of applied peptide bound at 200 cm h −1 to give an operating capacity of ∽90 mgper dry g. Following desorption, recovery was ∽98% with some further purification of the peptide. © 1999 Society of Chemical Industry