Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1991-5-14
pubmed:abstractText
The thermal stability of type II collagen in various solvents is shown to depend on the ability of the solvent to form hydrogen bonds. Mixtures of water with 1-propanol, 2-propanol, 1,2-propanediol, tetrahydrofuran and acetonitrile effect the stability of the triple helix differently. The temperature of the triple helix coil transition of type II collagen in 50(v/v)% solvent mixture in 0.1% trifluoroacetic acid ranges from 34 degrees C for 1,2-propanediol to 22.5 degrees C for acetonitrile, compared to 38 degrees C in 0.1% trifluoroacetic acid and 41.5 degrees C at neutral pH. There is no correlation between the dielectric constants of the solvents and the decrease in thermal stability, indicating that electrostatic interactions play only a minor role in the stability of the triple helix. Acetonitrile and tetrahydrofuran destabilize the triple helix more than the solvents containing hydroxyl groups. For reversed-phase high performance chromatography 2-propanol is the solvent of choice, but temperature control is very important, because the interaction of the triple helix with the column matrix leads to an additional destabilization of the triple helix beyond the destabilization effect of the solvent. In acetonitrile, a solvent commonly used for reversed-phase high performance chromatography, the triple helix is completely denatured when eluted from a C18 column at room temperature.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0934-8832
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
331-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Analysis of the thermal stability of type II collagen in various solvents used for reversed-phase high performance chromatography.
pubmed:affiliation
Research Unit, Shriners Hospital for Crippled Children, Portland, OR.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't