Linked Life Data

10883281

Source:http://linkedlifedata.com/resource/pubmed/id/10883281

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-19
pubmed:abstractText
Further purification of commercial human serum albumin was studied on immobilized Ni(2+)-IDA composite membrane cartridge. Effect of pH on HSA binding capacity was examined. A lot of impurities in the commercial HSA had been removed by a single step purification with a recovery of more than 85% of the protein bound on membrane cartridge. The purified HSA was of comparable purity of that from Sigma company analyzed by capillary electrophoresis. The nickel ion retained in the protein solution could be removed efficiently with the N, N, N'-tris (carboxymethyl) ethylenediamine chelating membrane cartridge.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1000-3061
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
74-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
[Immobilized Ni(2+)-IDA metal chelating affinity membrane chromatography for purification of commercial human serum albumin].
pubmed:affiliation
National Chromatographic R & A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences.
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't