Linked Life Data

1818080

Source:http://linkedlifedata.com/resource/pubmed/id/1818080

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1992-7-13
pubmed:abstractText
Bovine muscle carbonic anhydrase III was purified to homogeneity by the strategy of rapid ion-exchange chromatography. The ionic exchanger used was CM-cellulose, and this is the first application of this technique on a cation exchanger. Nitrogen gas was used to pressurize the chromatographic column to accelerate the elution. The results show that proteins with high isoelectric points can also be purified in this way. The procedure is very time-saving compared with conventional chromatography, reducing the elution time five- to ten-fold. The proteins are in addition protected against oxidation by air.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
588
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Rapid ion-exchange chromatography for preparative separation of proteins. IV. Application to bovine carbonic anhydrase III from skeletal muscle.
pubmed:affiliation
IFM/Department of Chemistry, Linköping University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't