Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1977-10-20
pubmed:abstractText
Minor contaminants occasionally found in conventionally prepared rat serum albumin were easily and completely removed by concanavalin A-Sepharose chromatography. The unadsorbed fraction from a concanavalin A-Sepharose column contained albumin which was homogeneous on polyacrylamide gel electrophoresis. The recovery of albumin form rat serum was approximately 30%. Approximately 2% of the added protein obtained as an albumin peak in DEAE-cellulose chromatography was adsorbed on and eluted with alpha-methyl-D-glucoside from the concanavalin A-Sepharose column, and resolved into three components by gel electrophoresis. There was one major glycoprotein, possibly alpha 1-antitrypsin, and two minor proteins one of which was albumin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1293-7
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
An improved method for the purification of rat serum albumin: removal of contaminants by concanavalin A-Sepharose.
pubmed:publicationType
Journal Article