Linked Life Data

7316780

Source:http://linkedlifedata.com/resource/pubmed/id/7316780

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1982-2-25
pubmed:abstractText
Isoelectric focusing (IEF) of the apoproteins of triglyceride rich human serum lipoproteins gives rise to the separation of some 15-20 protein bands. Three of these bands have been isolated in pure form and were characterized as isoelectric species of beta 2-glycoprotein-I (beta 2G-I). To compare the amino acid composition of these polymorphic forms with a representative specimen of beta 2G-I from total serum it was also necessary to apply a novel isolation procedure using Rivanol, perchloric acid and Heparin-Sepharose affinity chromatography. With the possible exception of the Pro content, the three isoforms were chemically and immunochemically identical. The isoelectric points of the polymorphic forms were 5.75, 6.0 and 6.2. Their molecular weight was identical by SDS polyacryl amide gel electrophoresis (54 000 D).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0098-6127
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-15
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Studies on the composition of the protein part of triglyceride rich lipoproteins of human serum: isolation of polymorphic forms of beta 2-glycoprotein-I.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't