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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1991-10-31
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pubmed:abstractText |
Human erythrocyte porphobilinogen deaminase was isolated using ammonium sulphate fractionation and heat treatment, Sephadex G-25 and G-100 chromatography, di-ethylamino-ethyl anion-exchange chromatography, chromatofocusing over a pH gradient of 7-4 and, finally, hydrophobic interaction chromatography on a phenyl-Sepharose column. The enzyme appeared pure as judged by sodium-dodecylsulphate-polyacrylamide gel electrophoresis with silver staining, and yielded a 7 115-fold purification.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0256-9574
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
21
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pubmed:volume |
80
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
294-6
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading | |
pubmed:year |
1991
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pubmed:articleTitle |
Purification of human erythrocyte porphobilinogen deaminase.
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pubmed:affiliation |
Department of Medicine, University of Cape Town.
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pubmed:publicationType |
Journal Article
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