Document Detail

Abnormal interaction of the human apolipoprotein A-I variant [Lys107----0] with high density lipoproteins.
MedLine Citation:
PMID:  3936504     Owner:  NLM     Status:  MEDLINE    
Several isoforms of apoprotein A-I [apoA-I], the major apoprotein of high density lipoproteins [HDL], have been described. We compared the in vivo and in vitro properties of normal human apoA-I with those of apoA-I [Lys107----0]. Fluorescence and circular dichroic spectra showed that deletion of Lys107 decreases apoprotein self-association. In vivo metabolic studies in the rat indicated that the interaction of apoA-I [Lys107----0] with HDL was lower than normal. We conclude that deletion of Lys107 results in a reorganization of the apoprotein structure that decreases its potential to form hydrophobic associations.
G Ponsin; A M Gotto; G Utermann; H J Pownall
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  133     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1985 Dec 
Date Detail:
Created Date:  1986-02-12     Completed Date:  1986-02-12     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  856-62     Citation Subset:  IM    
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MeSH Terms
Apolipoprotein A-I
Apolipoproteins A / metabolism*
Chromatography, Gel
Circular Dichroism
Lipoproteins, HDL / metabolism*
Protein Binding
Rats, Inbred Strains
Spectrometry, Fluorescence
Grant Support
Reg. No./Substance:
0/Apolipoprotein A-I; 0/Apolipoproteins A; 0/Lipoproteins, HDL

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