Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-5-4
pubmed:abstractText
The destabilizing effect of a multidose preservative, benzyl alcohol, on IFN-gamma was investigated. Hydrogen-deuterium isotope exchange (HX) detected by mass spectrometry (MS) was used to detect tertiary structure changes and measure global unfolding rates. The experiments showed that tertiary structure changes previously reported using circular dichroism may involve only a limited portion of the protein with the hydrophobic core of the protein remaining intact. Protein unfolding rates measured by hydrogen exchange were very sensitive to benzyl alcohol concentration, and increased markedly when salt was also added. Dynamic light scattering and size-exclusion chromatography showed that a small fraction of the protein formed large aggregates during the first few days. Measurements at longer incubation times (up to 8 days) showed that a significant fraction of protein was trapped in a structure less protected from hydrogen exchange, but not completely unfolded. This fraction of protein may be responsible for the irreversible loss of activity observed in earlier studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-3549
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:1605-1617, 2004
pubmed:issnType
Print
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1605-17
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Benzyl alcohol-induced destabilization of interferon-gamma: a study by hydrogen-deuterium isotope exchange.
pubmed:affiliation
Department of Chemical Engineering, University of Virginia, 102 Engineer's Way, Charlottesville, Virginia 22904-4741, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't