Dynamic affinity chromatography of heavy meromyosin subfragment-1.
Heavy meromyosin subfragment-1 and its trinitrophenylated derivative have been chromatographed on immobilized ATP, ADP and adenosine 5'-(geta, gamma-imino) triphosphate affinity chromatography columns, in the presence and in the absence of Ng-2+ or Ca-2+.ma-32-P] ATP columns.  While the divalent cations had little effect on the chromatographic pattern in the case of the non-hydrolyzable ADP and adenosine 5' (beta, gamma-imino) triphosphate, they catalyzed splitting in the case of ATP and at the same time strongly increased the affinity of adsorption of the proteins.  The protein-elution and the Pi-release patterns were different for the native and the modified proteins.  These results have been interpreted in terms of protein binding to the various intermediates of the ATP hydrolysis reaction.
D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases / Q000032:analysis; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002846:Chromatography, Affinity; D004492:Edetic Acid; D007097:Imines; D008274:Magnesium / Q000494:pharmacology; D015879:Myosin Subfragments / Q000302:isolation & purification*; D009596:Nitrophenols; D010446:Peptide Fragments; D011134:Polysaccharides; D011188:Potassium / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits
D007097:Imines; D015879:Myosin Subfragments; D009596:Nitrophenols; D010446:Peptide Fragments; D011134:Polysaccharides; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium; D002118:Calcium