Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-6-8
pubmed:abstractText
The cause of excessive band broadening of protein samples in polymer phase partitioning by counter-current chromatography (CCC) was investigated. A simple rotary device was constructed to measure the mass transfer rates of five samples including potassium dichromate, methylene blue, lysozyme, ovalbumin and human serum albumin. The results indicated that the mass transfer rates of these samples are closely correlated with their molecular masses: the higher the molecular mass, the lower the mass transfer rate. These findings are also consistent with the partition efficiencies of these samples in the same solvent system by CCC. The beneficial effect of the Coriolis force demonstrated in protein separations by the toroidal coil centrifuge may be reasonably explained on the basis of the mass transfer resistance of protein molecules through the interface: we speculate that when the Coriolis force acts parallel to the effective coil segment it can produce large interfacial areas by dispersing the mobile phase into the stationary phase, thus accelerating the mass transfer rate of protein samples.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
802
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-83
pubmed:dateRevised
2009-1-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Toroidal coil counter-current chromatography study of the mass transfer rate of proteins in aqueous-aqueous polymer phase system.
pubmed:affiliation
Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
pubmed:publicationType
Journal Article