Linked Life Data

1252461

Source:http://linkedlifedata.com/resource/pubmed/id/1252461

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-5-10
pubmed:abstractText
Acrylamide gel electrophoresis in dodecyl sulfate solutions of Folch-Pi apoprotein shows several bands. The different components were separated by Biogel P-200 filtration and then reduced and carboxymethylated. A comparative study of the amino acid composition, N-terminal sequence and C-terminal amino acid of the different components led to the assumption that their primary sequences are similar. Evidence for a contamination of the protein by free amino acids might explain the difference in terminal groups found by us and by other groups. It has been shown that the purified components can polymerize independently of S-S bond formation or exchange. The polymerization products were found to resist dissociation by dodecyl sulfate. It has been suggested therefore that the differences in migration rates of the various components are related to their shape rather than to their molecular weight.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
420
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-31
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Study of the apoprotein of Folch-Pi bovine proteolipid. II. Characterization of the components isolated from sodium dodecyl sulfate solutions.
pubmed:publicationType
Journal Article