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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1977-10-20
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1293-7
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:893354-Animals,
pubmed-meshheading:893354-Chromatography, Affinity,
pubmed-meshheading:893354-Concanavalin A,
pubmed-meshheading:893354-Immunoelectrophoresis,
pubmed-meshheading:893354-Methods,
pubmed-meshheading:893354-Rats,
pubmed-meshheading:893354-Sepharose,
pubmed-meshheading:893354-Serum Albumin
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pubmed:year |
1977
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pubmed:articleTitle |
An improved method for the purification of rat serum albumin: removal of contaminants by concanavalin A-Sepharose.
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pubmed:publicationType |
Journal Article
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