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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1987-6-8
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pubmed:abstractText |
beta-glucuronidase was purified by affinity chromatography on thiophenyl-glucuronide coupled to Sepharose. The enzyme was more than 95% pure. This enzyme is a tetramer composed of identical 74 kDa monomers. The amino-terminal sequence determined was: NH2-Met-Leu-Arg-Pro-Val.
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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:month |
Feb
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pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
157-61
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading | |
pubmed:year |
1987
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pubmed:articleTitle |
One step purification of Escherichia coli beta-glucuronidase.
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pubmed:publicationType |
Journal Article
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