Source:http://linkedlifedata.com/resource/pubmed/id/10703051
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2000-3-24
|
| pubmed:abstractText |
The allene oxide synthase (AOS) was purified from corn (Zea mays) seeds to homogeneity and characterized partially. The corn AOS was a hemoprotein cytochrome P450 with a molecular weight and pI of 53,000 and 6.0, respectively. The corn AOS was found to be irreversibly inactivated by a substrate, 13-hydroperoxyoctadienoic acid. The rate of the enzyme inactivation was higher at low pHs.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0031-9422
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
53
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
319-23
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| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
2000
|
| pubmed:articleTitle |
Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds.
|
| pubmed:affiliation |
Faculty of Nutrition, Kobe Gakuin University, Hyogo, Japan.
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| pubmed:publicationType |
Journal Article
|