Ready separation of proteins from nucleoprotein complexes by reversible modification of lysine residues

Modification of proteins with citraconic anhydride altered the electrostatic relationship between cationic epsilon-NH3+ groups of lysine residues of proteins and anionic phosphate groups of nucleic acids, thereby destabilizing the nucleoprotein complex. This procedure facilitated the separation of p...

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Bibliographic Details
Published in:Biochemical journal 1980-10, Vol.191 (1), p.269-272
Main Authors: Shetty, J K, Kinsella, J E
Format: Article
Language:English
Subjects:
Citraconic Anhydrides
Fungal Proteins - isolation & purification
Hydrogen-Ion Concentration
Lysine
Methods
Nucleoproteins
Saccharomyces cerevisiae - analysis
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Summary:Modification of proteins with citraconic anhydride altered the electrostatic relationship between cationic epsilon-NH3+ groups of lysine residues of proteins and anionic phosphate groups of nucleic acids, thereby destabilizing the nucleoprotein complex. This procedure facilitated the separation of proteins from nucleic acids at pH4-4.2. The modifying groups were then deacylated from the proteins under acidic conditions (pH3-6) at 30 degrees C.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1910269