Zobrazeno 1 - 5
of 5
pro vyhledávání: '"David W. Toome"'
Autor:
Navin D. Pathirana, S.J. Wheeler, David W. Toome, Jones Russell Mark, Peter R. Levison, Michael Streater, Stephen E. Badger
Publikováno v:
Journal of Chromatography A. 702:59-68
The effectiveness of a clean-in-place procedure involving treatment with 0.5 M NaOH for 16 h at room temperature has been examined following process-scale chromatography of 1.85 kg hen egg-white proteins on the DEAE-cellulose, Whatman Express-Ion Exc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d750f04f60c2b876e7dc44c29041e7e6
https://doi.org/10.1016/0021-9673(94)00991-h
https://doi.org/10.1016/0021-9673(94)00991-h
Publikováno v:
Journal of Chromatography A. 658:419-428
The scale-up of the separation of hen egg-white proteins was investigated using Whatman DEAE-cellulose/D856, a fast-flowing microgranular anion-exchange cellulose. Under suitable conditions the maximum binding capacity for ovalbumin was determined to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad2413c61b3231d793572ecba8a5f413
https://doi.org/10.1016/0021-9673(94)80032-4
https://doi.org/10.1016/0021-9673(94)80032-4
Autor:
Edward T. Butts, Mark L. Koscielny, Stephen E. Badger, Linda Lane, David W. Toome, Peter R. Levison
Publikováno v:
Journal of Chromatography A. 590:49-58
The scale-up of the separation of hen egg-white proteins has been investigated using Whatman DE92 anion-exchange cellulose. Having developed suitable chromatographic conditions, a maximum binding capacity of 100 mg protein/ml packed DE92 was determin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e673706914fca214055cf54d04d684b8
https://doi.org/10.1016/0021-9673(92)87005-s
https://doi.org/10.1016/0021-9673(92)87005-s
Publikováno v:
Separations for Biotechnology 2 ISBN: 9789401068390
Whatman DE52 (tertiary amine substituted anion-exchange cellulose) has been shown to exhibit fast kinetics of adsorption and high capacity for proteins of molecular mass up to 670 kDa. These features lend themselves to process-scale use and we have i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40b094e774cadbe8abb9ad5f3c9b57cf
https://doi.org/10.1007/978-94-009-0783-6_41
https://doi.org/10.1007/978-94-009-0783-6_41
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