Abstract:
:Stability of four dissimilar basic proteins (chymotrypsinogen A, ribonuclease A, cytochrome c, lysozyme) in the complex with four polyanions (heparin, poly(vinylsulfate), poly(4-styrene-sulfonate), Nafion) has been studied by differential scanning calorimetry. The polyanions were chosen because of their different charge density and hydrophobicity. Relative hydrophobicity of polyanions have been compared by three different parameters: (i) partition coefficient determined in octanol/water system, (ii) electrocapillary curves obtained by the method of controlled convection, and (iii) change in absorbance of small cationic amphiphilic molecule, aminoacridine, due to interaction with polyanion. Our results suggest that stability of proteins in the complex with polyanions negatively correlate with charge-related properties of the proteins such as isoelectric point and surface charge density and hydrophobicity of the polyanions.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Sedlák E,Fedunová D,Veselá V,Sedláková D,Antalík Mdoi
10.1021/bm900480tsubject
Has Abstractpub_date
2009-09-14 00:00:00pages
2533-8issue
9eissn
1525-7797issn
1526-4602journal_volume
10pub_type
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