Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-5-15
pubmed:abstractText
Oleosins are amphipathic proteins associated with oil bodies in seeds. We purified the major 16,500 peanut oleosin by preparative SDS-PAGE. Autoradiography after SDS-PAGE separation of the iodinated oleosin revealed covalently bound oligomers with Mr of 21,000, 33,000, 44,000 and 51,000. The strong capacity of these oligomers to form aggregates and to be incorporated into large-sized detergent micelles was demonstrated by gel permeation and isoelectric focusing. A 50% ethanol concentration was necessary to elute the 16,500 oleosin from octyl groups in hydrophobic interaction chromatography showing its natural tendency to interact with lipid acyl chains. This oligomerization behavior in aqueous solution is an indirect reflection of the interactions that occur in the oil body.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1387-2273
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
706
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Characterization of the oligomeric behavior of a 16.5 kDa peanut oleosin by chromatography and electrophoresis of the iodinated form.
pubmed:affiliation
Laboratoire de Pathologie Cellulaire et Moléculaire en Nutrition, EP CNRS 0616, Faculté de Médecine, Vandoeuvre-lès-Nancy, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't