Linked Life Data

4112

Source:http://linkedlifedata.com/resource/pubmed/id/4112

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-7-6
pubmed:abstractText
A comparison of the conformation of Folch-Pi apoprotein in organic solvent and in aqueous solutions has been made by ESR, infrared and circular dichroism spectroscopy studies. Electrophoresis and ultracentrifugation have been carried out in order to correlate molecular weight and charge of the molecule with its conformation. It appears that the protein is monomeric in organic solution. In water, only one component is present but the molecules behave as a polydisperse system of associating molecules. Hydrophobic interacitons seem to be important for this polymerisation which does not appear to be accompanied by the formation of beta-structure. After the transfer of the protein from organic solution to water, the ESR spectra of the protein labelled on the free SH groups show an heterogeneity in the motional environment of the label which permits to assume that different areas of association exist in the polymeric molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
427
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
44-56
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
A study of Folch-Pi apoprotein. II. Relation between polymerization state and conformation.
pubmed:publicationType
Journal Article