[The competition of serum amyloid protein and apoprotein E for binding with human serum albumin].
The relationship between the concentration of serum amyloid protein (SAP) isolated from human serum and the parameters of the protein elution during gel-filtration and alos with the efficiency of Ca(2+)-dependent SAP binding with sepharose 4B was studied. The dissociation of the SAP oligomeric form in solution and the interaction of the protein with human serum albumin with fully reduced S--S bridges due to the introduction of the additional hydrophobic surface was shown. Apoprotein E isolated from human plasma very-low-density lipoproteins replaced SAP in the complex with albumin.
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D001057:Apolipoproteins E / Q000032:analysis / Q000097:blood* / Q000302:isolation & purification; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004305:Dose-Response Relationship, Drug; D016650:Fluorescein-5-isothiocyanate; D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding; D012709:Serum Albumin / Q000032:analysis / Q000378:metabolism*; D000685:Serum Amyloid A Protein / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*
D001057:Apolipoproteins E; D012709:Serum Albumin; D000685:Serum Amyloid A Protein; D016650:Fluorescein-5-isothiocyanate
Konkurentsiia syvorotochnogo amiloidnogo belka i apobelka E za sviazyvanie s syvorotochnym al'buminom cheloveka.