Anion exchange chromatography of proteins leads to induction of DNA-binding activity in them
Rott, G.M.; Podgorodnichenko, V.K.; Rozhinskaia, I.V.; Novikova, I.S.
Molekuliarnaia Biologiia 28(2): 383-391
1994
ISSN/ISBN: 0026-8984 PMID: 8183270 Document Number: 435907
The present work is devoted to investigation of the acquired DNA-binding activity of several proteins, such as bovine serum albumin, myoglobin, and collagens in different conformational states (native, denatured, and gelatin) following their anion exchange chromatography. Induction of DNA-binding activity, as shown, is natural phenomenon common in protein treatment on positively charged matrix. Obviously, anion exchange chromatography of proteins results in their structural conformational changes. It was suggested that the DNA-binding activity of activated proteins is based on the ability of the protein molecule to accept additional protons upon contact with the anion exchanger. This hypothesis is confirmed by the inhibition of the interaction of activated protein with DNA in the presence of Na-EDTA.