Linked Life Data

8507644

Source:http://linkedlifedata.com/resource/pubmed/id/8507644

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1993-7-9
pubmed:abstractText
The secondary structure of the human low-density lipoprotein (LDL) apo B-100 fragment embedded in the lipid domain of the particle has been investigated by Fourier transform attenuated total reflection infrared spectroscopy (FTIR-ATR). The solvent-exposed region of the protein was hydrolyzed by using different proteases (alpha-chymotrypsin, trypsin, proteinase K) for incubation times varying between 24 min and 48 h. Analysis of the FTIR-ATR spectra after repurification of the digested LDL particle indicates the same trend for all the hydrolysis conditions tested: the peptides remaining associated with the particle are rich in beta-sheet structure. Dichroism spectra reveal that at least part of the beta-sheets is associated with the phospholipid component of the particle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6104-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy.
pubmed:affiliation
Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't