Dynamic affinity chromatography of heavy meromyosin subfragment-1 |
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Authors: | Avraham Oplatka Raphael Lamed Andras Muhlrad |
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Institution: | Department of Polymer Research, The Weizmann Institute of Science, Rehovot, Israel |
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Abstract: | Heavy meromyosin subfragment-1 and its trinitrophenylated derivative 3ave been chromatographed on immobilized ATP, ADP and adenosine 5′-(β,γ-imino)triphosphate affinity chromatography columns, in the presence and in the absence of Mg2+ or Ca2+. Splitting of bound ATP was followed by using γ-3 2P]ATP columns. While the divalent cations had little effect on the chromatographic pattern in the case of the non-hydrolyzable ADP and adenosine 5′(β,γ-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. |
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Keywords: | heavy meromyosin S-1 heavy meromyosin subfragment 1 agarose?ATP agarose ?adipic acid hydrazide?ATP AMP-P(NH)P adenosine 5′-(β γ-imino)triphosphate |
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