Molecular Basis of Motility by J. C. Rüegg (auth.), Ludwig M. G. Heilmeyer Jr., J. C.

By J. C. Rüegg (auth.), Ludwig M. G. Heilmeyer Jr., J. C. Rüegg, Th. Wieland (eds.)

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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.

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