Linked Life Data

6774755

Source:http://linkedlifedata.com/resource/pubmed/id/6774755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-12-16
pubmed:abstractText
Pigeon plasma high density lipoproteins (HDL) were isolated by ultracentrifugation between the densities of 1.063 and 1.21 g/ml. Gel filtration of delipidated HDL in 5 M guanidine-HCl on Sephadex G-150 yielded a major fraction which eluted at the same position as human apolipoprotein A-I isolated from HDL. In SDS-gel electrophoresis, the isolated apolipoprotein co-migrated with human apolipoprotein A-I with a molecular weight of approx. 28 000. The amino acid composition was similar to the apolipoprotein A-I isolated from human and hen plasma. The isolated apolipoprotein from pigeon plasma had therefore been designated as apolipoprotein A-I. As judged by circular dichroism (CD), the apolipoprotein A-I displayed a maximum mean residue ellipticity of approx. -3 000 at 222 nm while at concentrations greater than 0.2 mg/ml. Calculations of alpha-helicial content gave values of 85%. Lowering the concentration of apolipoprotein A-I was found to concomitantly decrease the ellipticity (absolute value) suggesting that there was some conformational change when the apolipoprotein A-I concentration varied. The isolated pigeon apolipoprotein A-I was found bound to the phospholipid (dimyristoyl phosphatidylcholine) and there was no significant conformational change upon lipid binding as judged by CD. Under the same experimental conditions, human apolipoprotein A-I exhibited a drastic conformational change by increasing its helicity in the presence of phospholipid. The helical content of human apolipoprotein A-I was increased from 48 to 85%. This finding suggests that the apolipoprotein may not necessarily increase its helical content during lipid binding. Moreover, immunochemical studies showed that rabbit antiserum prepared against pigeon apolipoprotein A-I could partially react with human apolipoprotein A-I determined by quantitative radioimmunoassay.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
620
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
100-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Physical, chemical, and immunochemical studies of apolipoprotein A-I from pigeon plasma high density lipoproteins.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.