Linked Life Data

9989282

Source:http://linkedlifedata.com/resource/pubmed/id/9989282

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-3-4
pubmed:abstractText
Two fatty acid hydroperoxide lyases (HPO lyase I and II) were purified to apparent homogeneity from etiolated hypocotyls of sunflower (Helianthus annuus L.) by a combination of ion-exchange, hydrophobic interaction, and gel filtration chromatography. The two HPO lyases were separated during the hydrophobic interaction chromatography step, with HPO lyase I more hydrophilic than HPO lyase II. The estimated M(r) of both native HPO lyases was determined by gel filtration to be 200,000 and SDS-PAGE in the presence of 100 mM dithiothreitol showed that the enzyme was composed of a single 53 kDa peptide, suggesting that the enzyme exists as a tetramer in vivo. HPO lyase was also abundant in the cotyledons and green leaves. HPO lyases I and II from hypocotyl metabolized 13-hydroperoxylinoleic acid and 13-hydroperoxylinolenic acid to the same extent, but the green leaf enzyme was more than ten-fold more active with 13-hydroperoxylinolenic acid than 13-hydroperoxylinoleic acid. A difference spectrum between CO-bound and CO-unbound dithionite-reduced HPO lyase I showed an absorbance maximum at 452 nm, indicating that it was a cytochrome P450-type enzyme. The activities of HPO lyase I and II were significantly inhibited by nordihydroguaiaretic acid, sulfhydryl reagents, and piperonylbutoxide, which is a cytochrome P450 inhibitor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
1436
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
531-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
The purification and characterization of fatty acid hydroperoxide lyase in sunflower.
pubmed:affiliation
Northern Crop Science Laboratory, U.S. Department of Agriculture, Fargo, ND 58105, USA.
pubmed:publicationType
Journal Article