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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
|
pubmed:dateCreated |
1979-3-29
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pubmed:abstractText |
The purification was begun with acetone precipitation of minced brain tissue with subsequent proteinase extraction with 0.2 M sodium formate buffer (pH 3.5), reprecipitation with acetone and dialysis. Chromatographic separation on Sephadex G-200, DEAE-Sephadex A-50 and CM-cellulose was carried out in that order. Upon ion-exchange chromatography multiple forms of acid proteinases emerged; two of them were obviously identical with cathepsin D (EC 3.4.23.5), and two of them exhibited properties of cathepsin B (EC 3.4.22.1).
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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:issn |
0302-4369
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
B32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
727-32
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:735639-Animals,
pubmed-meshheading:735639-Brain,
pubmed-meshheading:735639-Cattle,
pubmed-meshheading:735639-Chromatography, DEAE-Cellulose,
pubmed-meshheading:735639-Chromatography, Gel,
pubmed-meshheading:735639-Chromatography, Ion Exchange,
pubmed-meshheading:735639-Endopeptidases
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pubmed:year |
1978
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pubmed:articleTitle |
Purification of acid proteinases from calf brain.
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pubmed:publicationType |
Journal Article
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