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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1994-12-30
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pubmed:abstractText |
Mouse complement component C7 was purified from serum by a sequential procedure of fractionation precipitation by ammonium sulfate, followed by DE-52 anion exchange chromatography. Protein G affinity column chromatography, Mono S cation exchange chromatography and Superdex 200 gel filtration. The final product contained a highly purified mouse C7 component showing a single band on SDS-PAGE at the apparent Mrs of 90 kDa and 100 kDa under non-reduced and reduced conditions respectively. The yield of C7, which was measured by the biological activity, was 7.0%
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1759
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
163-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7983377-Animals,
pubmed-meshheading:7983377-Chemical Fractionation,
pubmed-meshheading:7983377-Chromatography,
pubmed-meshheading:7983377-Complement C7,
pubmed-meshheading:7983377-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7983377-Mice,
pubmed-meshheading:7983377-Mice, Inbred DBA
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pubmed:year |
1994
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pubmed:articleTitle |
Isolation of mouse complement component C7.
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pubmed:affiliation |
Department of Clinical Laboratory Medicine, Ehime University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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