Linked Life Data

8674512

Source:http://linkedlifedata.com/resource/pubmed/id/8674512

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-8-15
pubmed:abstractText
In other systems, proteins have been shown to alter the molecular structures of lipids in the cell membrane bilayer. We wished to determine if proteins altered the structure of lens lipids. The structure of lipid hydrocarbon chains in urea purified human lens membrane vesicles containing intrinsic, hydrophobically bound proteins was compared to the structure of lipids in vesicles without protein. Fourier transform Raman spectroscopy was used to characterize lipid and protein structure. To study lipid interactions with extrinsic, surface bound proteins, the lipid structure was compared in bovine lipid vesicles with and without alpha-crystallin bound to the surface of the membrane. Lipid structure was studied using Fourier transform infrared spectroscopy. No change in lipid structure was detected even at protein/lipid weight ratios of two to one. Human lens intrinsic proteins contained a high amount of a helical structure (60%), but did not alter hydrocarbon chain interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-53
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Lipid-protein interactions in human and bovine lens membranes by Fourier transform Raman and infrared spectroscopies.
pubmed:affiliation
Department of Ophthalmogy and Visual Sciences, University of Louisville, KY 40292, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't