Document Detail


Chromatographic separations of serum proteins on immobilized metal ion stationary phases.
MedLine Citation:
PMID:  2619035     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The separation of proteins on stationary phases consisting of a bound organic chelator and a chelated divalent transition metal has been studied as a function of (A) metal ion species; (B) mobile phase composition and pH; and (C) anion and cation concentration. Optimum separation was observed at alkaline pH on chelated nickel stationary phases. Ammonium and Tris salts reduced the affinity of the metal chelate packing for serum proteins. Halide ions caused the proteins to be more strongly bound to the stationary phase. High salt concentrations had only a small effect on the binding of serum proteins in the absence of amine containing buffers or salts. It was also observed that the ease of elution and the recovery of protein were dependent on pH and upon the presence of halides. The general order of elution of serum proteins, based on isoelectric focusing, was independent of metal ion species and elution conditions, suggesting that a single mechanism or a unique sequence of mechanisms was operative. The results suggest that ligand exchange is the major mechanism of separation under basic conditions and that hydrophobic effects are the result of the competition of nonnitrogen ions with ammonium ions or amines for ligand binding sites modifying or participating in protein binding. Protein binding studies under weak acidic conditions are also presented although the mechanism responsible for protein binding is unclear.
Authors:
S A Margolis; A J Fatiadi; L Alexander; J J Edwards
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Analytical biochemistry     Volume:  183     ISSN:  0003-2697     ISO Abbreviation:  Anal. Biochem.     Publication Date:  1989 Nov 
Date Detail:
Created Date:  1990-03-08     Completed Date:  1990-03-08     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0370535     Medline TA:  Anal Biochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  108-21     Citation Subset:  IM    
Affiliation:
Organic Analytical Research Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899.
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MeSH Terms
Descriptor/Qualifier:
Blood Protein Electrophoresis / methods*
Blood Proteins / isolation & purification*
Buffers
Chromatography, Affinity / methods
Cobalt
Copper
Electrophoresis, Gel, Two-Dimensional
Humans
Hydrogen-Ion Concentration
Imino Acids
Isoelectric Focusing
Manganese
Metals*
Nickel
Osmolar Concentration
Salts
Sepharose
Zinc
Chemical
Reg. No./Substance:
0/Blood Proteins; 0/Buffers; 0/Imino Acids; 0/Metals; 0/Salts; 142-73-4/iminodiacetic acid; 7439-96-5/Manganese; 7440-02-0/Nickel; 7440-48-4/Cobalt; 7440-50-8/Copper; 7440-66-6/Zinc; 9012-36-6/Sepharose

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


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