Parallel response of myofibrillar contraction and relaxation to four different nucleoside triphophates.

The Mg chelates of ITP, GTP, and UTP in addition to that of ATP were shown to be capable of causing complete relaxation of myofibrils as indicated by the complete inhibition of syneresis and the reduction of the NTPase activity to that of isolated myosin. For ITP and GTP the required concentrations were about 100 times higher than those for ATP, whereas UTP was maximally effective also in low concentrations (0.2 mM). For all NTP's the concentrations for relaxation were related to those necessary for contraction so that NTP concentrations which gave 80-90% maximal NTPase activity in the presence of Ca caused complete relaxation in the absence of Ca. Thus, these experiments do not support the view that relaxation is caused by the binding of NTP to a special inhibitory site but are quite compatible with the idea that relaxation depends on the extent to which the hydrolytic site is saturated with NTP. The Ca concentration required for contraction depends on the nature of the NTP base and its concentration; it is lower for ITP than for ATP and decreases with decreasing concentrations of ITP.