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Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1979-10-17
|
pubmed:abstractText |
Guanylate cyclase activity is present in crude E. coli extract. Guanylate cyclase has been purified 3500 fold from this extract, through ammonium sulfate fractionation, DEAE-cellulose chromatography. Sephadex G-75 gel-filtration and polyacrylamide gel preparative microelectrophoresis. During the purification a guanylate cyclase inhibitor has been separated.
|
pubmed:language |
fre
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0037-9026
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
172
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
860-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading | |
pubmed:year |
1978
|
pubmed:articleTitle |
[Guanylate cyclase in Escherichia coli. I. Purification of the enzyme and evidence for an inhibitor].
|
pubmed:publicationType |
Journal Article,
English Abstract
|