Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1986-9-16
pubmed:abstractText
Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates. They can be used as stationary phases in high-performance affinity chromatography of thrombin. Under isocratic conditions, thrombin is strongly adsorbed on the resins when the sodium chloride concentration is lower than 0.5 M. The bound enzyme can be selectively desorbed when the salt concentration is raised to about 1.2 M. With a linear salt gradient, the specific elution of thrombin can be effected with a high recovery of its enzymatic activity. The decomposition products of thrombin, when treated with sodium dodecyl sulphate, are not retained by the stationary phase. The effects of the flow-rate and salt gradient slope on the adsorption and desorption of alpha-thrombin demonstrate the importance of kinetic parameters.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
359
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-7
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
High-performance affinity chromatography of human thrombin on modified polystyrene resins.
pubmed:publicationType
Journal Article