Linked Life Data

18072302

Source:http://linkedlifedata.com/resource/pubmed/id/18072302

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-12-11
pubmed:abstractText
The Folch-Pi proteolipid has been isolated from bovine white matter and characterized with respect to phospholipid and glycolipid composition. The protein-lipid complex has been solubilized in aqueous reverse micelles of di(2-ethylhexyl) sodium sulfosuccinate and isooctane. Solubilization of this otherwise water-insoluble proteolipid requires small amounts of water, the percent of solubility being maximum for a low molar ratio of water to surfactant (Wo = 5.6). Unlike hydrophilic proteins, the extent of incorporation into the micellar system is negligible at 50 mM surfactant and reaches 90Vo only at 300 mM. However, the conformation of the proteolipid in reverse micelles as studied by fluorescence emission spectroscopy and circular dichroism was not affected by variations of the surfactant concentration. These results are consistent with the peculiar properties of the aqueous environment of the proteolipid within the reverse micelles and may reflect the membrane-like character of these bio-assemblies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
172
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
343-7
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Solubilization and insertion into reverse micelles of the major myelin transmembrane proteolipid.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale (U 221), Centre National de la Recherche Scientifique (ER 64), Unité d'Enseignement et de Recherche Biomédicale des Saints Pères, 45 rue des Saints Pères, 75270 Paris Cédex 06, France.
pubmed:publicationType
Journal Article