Document Detail


Hydrophobic interactions of the apo-Gln-I polypeptide component of human high density serum lipoprotein.
MedLine Citation:
PMID:  165177     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Apo-Gln-I, the major polypeptide component of human serum high density lipoprotein, has four noninteracting hydrophobic sites which associate with alkanes, anionic detergents, and cationic detergents. Hexane and octane bind to these sites with association constants of 6.8 times 10-2 and 1.8 times 10-4 liters/mol, respectively, and compete with the anionic detergent, sodium dodecyl sulfate (C12OSO3-minus), at low detergent ligand binding ratios (i.e. smaller than or equal to 1.0 mol of C12OSO3-minus per mol of protein). At higher detergent binding ratios (larger than 2 mol of C12OSO3-minus per mol of protein) the polypeptide cooperatively binds alkanes and a conformational change is induced.
Authors:
W L Stone; J A Reynolds
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  250     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1975 May 
Date Detail:
Created Date:  1975-07-24     Completed Date:  1975-07-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3584-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Alkanes
Apoproteins* / blood
Binding Sites
Glucosamine
Humans
Kinetics
Ligands
Lipoproteins, HDL* / blood
Protein Binding
Sodium Dodecyl Sulfate
Spectrophotometry, Ultraviolet
Thermodynamics
Ultracentrifugation
Chemical
Reg. No./Substance:
0/Alkanes; 0/Apoproteins; 0/Ligands; 0/Lipoproteins, HDL; 151-21-3/Sodium Dodecyl Sulfate; 3416-24-8/Glucosamine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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