Effect of trinitrophenylation on the correlation between ATPase activity and superprecipitation of skeletal actomyosins.
The results of this work have shown that the actin-induced increase of the presteadystate extraphosphate production is depressed in the case of the trinitrophenylated myosin A. At the same time the onset of superprecipitation is delayed and the rate of turbidity change of the trinitrophenylated synthetic actomyosins is depressed significanylt. The results of these experiments failed to demonstrate any correlation between the steadystate ATPase activity of myosin A or actomyosin enzyme and the onset and rate of the superpricipitation reactions. The results of this study seem to indicate that the time resolution of the instruments used to monitor the turbidity changes during the superprecipitation reaction may be an important factor in the proper evaluation of the experimental results.
D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D011232:Chemical Precipitation; D004533:Egtazic Acid / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D009578:Nitrobenzenes / Q000494:pharmacology*
D000199:Actins; D009578:Nitrobenzenes; D004533:Egtazic Acid; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium