Linked Life Data

3996606

Source:http://linkedlifedata.com/resource/pubmed/id/3996606

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-7-25
pubmed:abstractText
Divinylsulphone-activated agarose to which mercaptoethanol is coupled showed very selective group adsorption of human serum proteins, in particular the immunoglobulins. The adsorption increases markedly in the presence of high concentrations of neutral water-structure forming salts and is distinct from adsorptions based on hydrophobic interaction. A characteristic feature of this new type of adsorbent is the structure of the groups attached to the polymer, P, i.e., R-S-CH2-CH2-SO2-CH2-CH2-O-P, where R is a small aliphatic residue. Our results indicate that the thioether sulphur and the adjacent sulphone group act cooperatively and are apparently necessary to maintain the distinct behaviour of such absorbents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
306-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Thiophilic adsorption--a new method for protein fractionation.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't