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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1992-5-7
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pubmed:abstractText |
Four forms of bovine adrenodoxin with modified amino-termini obtained by direct expression of cDNAs in Escherichia coli are Ad(Met1), Ad(Met-1), Ad(Met-12), and Ad(Met6). The shoulder numbers represent the site of translation initiator Met at the amino-termini. The adrenodoxins, except for Ad(Met-1), were purified from the cell lysate and the ratios of A414-to-A276 of the purified proteins were over 0.92. NADPH-cytochrome c reductase activities of the three forms of adrenodoxin in the presence of adrenodoxin reductase were the same as that of purified bovine adrenocortical adrenodoxin. However, as cytochrome P-450SCC reduction catalyzed by Ad(Met6) was about 60% of that by Ad(Met1), the contribution of the amino-terminal region for the electron transfer or binding to cytochrome P-450SCC would need to be considered.
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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 |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
300
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
208-12
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1555645-Adrenodoxin,
pubmed-meshheading:1555645-Amino Acid Sequence,
pubmed-meshheading:1555645-Animals,
pubmed-meshheading:1555645-Base Sequence,
pubmed-meshheading:1555645-Catalysis,
pubmed-meshheading:1555645-Cattle,
pubmed-meshheading:1555645-Cloning, Molecular,
pubmed-meshheading:1555645-Escherichia coli,
pubmed-meshheading:1555645-Genetic Vectors,
pubmed-meshheading:1555645-Molecular Sequence Data,
pubmed-meshheading:1555645-Recombinant Proteins,
pubmed-meshheading:1555645-Structure-Activity Relationship
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pubmed:year |
1992
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pubmed:articleTitle |
Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino-terminal regions.
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pubmed:affiliation |
Department of Microbiology, Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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