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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1987-2-13
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pubmed:abstractText |
Technological and methodological advances in the techniques of structural and biological studies of proteins have reduced the required amount of sample. In conjunction with these advances, high-performance liquid chromatography (HPLC) has emerged as a technique of high utility for the purification of complex molecules. Using a combination of size-exclusion and reversed-phase HPLC and ionic buffers containing sodium dodecyl sulfate, the red cell membrane-associated high-molecular-weight polypeptide spectrin and its subunits have been purified. The system described in this paper is fast, reproducible and quantitative.
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pubmed:grant | |
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 |
Nov
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pubmed:issn |
0021-9673
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
369
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-64
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1986
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pubmed:articleTitle |
Purification of spectrin and its subunits by high-performance liquid chromatography.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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