Linked Life Data

18080342

Source:http://linkedlifedata.com/resource/pubmed/id/18080342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-4-2
pubmed:abstractText
Although virus filtration is now an integral part of the overall viral clearance strategy for the purification of many commercial therapeutic proteins, there is currently little understanding of the factors controlling the performance of the virus filters. The objective of this study was to examine the effects of solution pH on protein transmission and capacity during virus filtration. Data were obtained using bovine serum albumin as a model protein with Viresolve 180 membranes oriented with both the skin-side up and skin-side down. Membranes were also characterized using dextran sieving measurements both before and after protein filtration. Membrane capacity and protein yield were minimal at the protein isoelectric point, which was due to the greater degree of concentration polarization associated with the smaller protein diffusion coefficient at this pH. In contrast, the actual protein sieving coefficient was maximum at the protein isoelectric point due to the absence of any strong electrostatic exclusion under these conditions. The yield and capacity were both significantly greater when the membrane was oriented with the skin-side down. These results provide important insights into the effects of solution conditions on the performance of virus filtration membranes for protein purification.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1097-0290
pubmed:author
pubmed:copyrightInfo
Copyright 2007 Wiley Periodicals, Inc.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
108-17
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Effect of solution pH on protein transmission and membrane capacity during virus filtration.
pubmed:affiliation
Department of Chemical Engineering, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
pubmed:publicationType
Journal Article, Evaluation Studies