By J. C. Rüegg (auth.), Ludwig M. G. Heilmeyer Jr., J. C. Rüegg, Th. Wieland (eds.)
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Extra resources for Molecular Basis of Motility
1 The experiment described in Table 2 was repeated using the same subfragment 1 preparatio~ but with no actin present. The 2 s quenching and 'cold chase' measurements were made as described previously. The catalytic centre activity increased linearly with actin concentration in the range 0-3 mg/ml F-actin - a result consistent with other steady-state kinetic studies (Moos, 1972). Marston and Weber (1975) have estimated the actin-subfragment 1 dissociation constant as about 10- 8 M. This means the concentration of free subfragment 1 in the experiment of Table 2 was less than 10- 7 M.
III. Glycerinated Fibres as a Model of Muscular Contraction The treatment of muscle fibres with 50% glycerol at -20 0 C destroys the membranes and releases the soluble proteins of the sarcoplasm. Glycerinated fibres from rabbit psoas will contract when MgATP is added under the correct ionic conditions (Szent-Gyorgyi, 1949). Thus glycerinated preparations may be used to examine the effects of chemical modifications to substrate or protein. , 1964). These muscle fibres also give rise to a detailed X-ray low-angle diffraction pattern which makes them very suitable for our present studies.
P. are rate-limiting. J. e-p-e I I I o-p-o o o , ? e o Eq. (3) describes a possible mechanism for intermediate exchange. 0 and e differentiate oxygen atoms arising from H2 0 and ATP respectively R-f-e, R and O-f-O represent ATP, ADP and Pi respectively. k rot is the rate of the process which occurs to allow oxygen atoms emanating from ATP to be eliminated in the reverse reaction. The rate constant k-3 [see Eq. (1)] may directly control the rate of intermediate exchange. 35 s. Approximately one atom has exchanged 45 Table 1.