By Rhea J. C. Levine (auth.), Gerald H. Pollack, Haruo Sugi (eds.)

Prior to the emergence of the sliding filament version, contraction theories were in abundance. within the absence of the types of structural and biochemical details on hand this day, it's been an easy topic to invest concerning the attainable ways that pressure iteration and shortening could happen. the appearance of the sliding filament version had a right away effect on those theories; inside of a number of years they fell by means of the wayside, and a focus was once redirected in the direction of mechanisms wherein the filaments will be pushed to slip through each other. when it comes to settling on the riding mechanism, the pivotal observa­ tion used to be the electron micrographic indentification of cross-bridges extending from the thick filaments. It used to be really certainly assumed that such bridges, which had the facility to separate ATP, have been the molecular cars, i.e., that they have been the websites of mechanochemical transduction. Out of this presumption grew the cross-bridge version. during which filament sliding is presumed to be pushed through the cyclic interplay of cross-bridges with complementary actin websites positioned alongside the skinny filaments.

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We also measured filament lattice spacing directly by X-ray diffraction of the fibrils. Our new measurements with these methods, taken here from papers submitted and in preparation (Reedy and Lucaveche, 1983) convinced us that the discrepancy between filaments and fibrils is a definite finding in IFM, and can be demonstrated in material from vertebrate skeletal muscle (VSkM) as well. tWe propose "AO-band"as an easily recognized abbreviation for "filament overlap zone", to replace the less obvious "A·-zone" (Huxley and Hanson, 1957).

Myofilament Substructure 25 Figure 2: Schematic diagram of Fig. 1 showing the possible spatial relation of actin and myosin Sl in actin-tropomyosin-S1. In (a), (b), (c) and (d), domain A(Al+A2), domain B(Bl+B2), subdomains Bl+Al' and subdomains Bl+Al are assumed to be actin, respectively. Note that in each of four arrangements, Sl and actin make morphological contact at two or more sites and in some cases Sl binds two actin molecules. The domain A is lower in density in actin-tropomyosin-S1 than in actin-S1.

17 as found by Huxley and Hanson (1957). but needs a few more supporting experiments before we are prepared to insist on it. Among these must be satisfactory control experiments that rule out both squeezing and penetration by matching fluids. like our controls with IFM. Nonetheless. our preliminary mass thickness profiles. from EMs of unstained rabbit sarcomeres like that published from an insect sarcomere {Reedy et al.. 20. 31 is the H:I ratio expected for 3 myosin/crown on the basis of filament masses alone.

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