[Acetate kinase chromatography on agarose derivatives].
Acetate kinase from E. coli K-12 was studied chromatographically on omega-aminoalkyl polysacharide sorbents. The dependence of the protein sorption-desorption on ionic strength and the effect of pH on the acetate kinase sorption were studied. The increase in the ionic strength caused a decrease in the amount of protein sorbed on the hexamethylenediamine- and chlorotriasinehexamethylenediamine sepharoses. On hexamethylenediamine-, octamethylenediamine- and dimethylhexamethylenediamine agaroses acetate kinase was adsorbed within the pH range of 6.5-9.0, whereas on the chlorotriasinehexamethylenediamine sepharose--at pH 6.5-8.0. The active protein was eluted at ionic strength of 0.14-0.17 M. Acetate kinase was not adsorbed on the carboxypropyonylaminohexyl sepharose within the pH range studied, i.e. 5.0-9.0 and was not adsorbed on hexamethylenediamine agarose at pH 4.0 and on chlorotriasinehexamethylenediamine sepharose--at pH 9.0. The mechanism of the enzyme-adsorbent interaction is discussed.
D000085:Acetates; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D010770:Phosphotransferases / Q000302:isolation & purification*; D012685:Sepharose
D000085:Acetates; D012685:Sepharose; D010770:Phosphotransferases
Khromatografiia atsieatkinazy na proizvodnykh agarozy.