By Rhea J. C. Levine (auth.), Gerald H. Pollack, Haruo Sugi (eds.)
ISBN-10: 1468447033
ISBN-13: 9781468447033
ISBN-10: 146844705X
ISBN-13: 9781468447057
Prior to the emergence of the sliding filament version, contraction theories were in abundance. within the absence of the categories of structural and biochemical info to be had this day, it's been an easy subject to invest concerning the attainable ways that stress new release and shortening could take place. the arrival of the sliding filament version had an instantaneous influence on those theories; inside a number of years they fell by means of the wayside, and a focus was once redirected in the direction of mechanisms during which the filaments will be pushed to slip through each other. when it comes to selecting the riding mechanism, the pivotal observa tion used to be the electron micrographic indentification of cross-bridges extending from the thick filaments. It was once relatively certainly assumed that such bridges, which had the power 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. within which filament sliding is presumed to be pushed by means of the cyclic interplay of cross-bridges with complementary actin websites positioned alongside the skinny filaments.
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90: 683-701. Myofilament Substructure 27 DISCUSSION KA WAI: Does your domain analysis change if you add small amounts of S-l instead of full amounts of S-l ? WAKABAYASHI: We're trying, but it is very difficult to get good symmetry when we partially decorate the thin filament. KAWAI: What happens if you add small quantities of troponin? WAKABAYASHI: We did not do that experiment yet. SUGI: Did you prepare the actin-S-1 complex with calcium or without calcium? WAKABAYASHI: The calcium concentration was not controlled with EGTA, so it's nominally free.
We recently devised another independent test. We used a Mettler-Paar density meter (accurate to 5-6 decimal places) to measure the density of the well-defined isopycnic band which IFM fibrils produce on self-forming gradients when centrifuged in Percoll of about 3-4% PE. 75. 0325 if they were 13% protein. 0425 if they were 17% protein. 0422). 0432). 048). 5%). rather than 13%. and concentration of myofibrillar proteins can be reliably found from RI. 18 ml/g. Protein Content of Vertebrate Muscle Cross-Bands Refractometry of the rabbit VSkM AD-band indicates a protein concentration of 18-19%.
Biochem. 90: 703-714. E. J. (1970). Three-dimensional reconstruction of Factin. thin filaments and decorated thin filaments. J. Mol. BioI. 50: 279-295. Mornet. • Bertrand. R.. Pantel. • Audemard. E. & Kassab. R. (1981). Structure of the actin-myosin interface. Nature 292: 301-306. Seymour. J. & O'Brien. J. (1980). The position of tropomyosin in muscle thin filaments. Nature 283: 680-682. Spudich. , Huxley. E. & Finch. T. (1972). Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin.
Contractile Mechanisms in Muscle by Rhea J. C. Levine (auth.), Gerald H. Pollack, Haruo Sugi (eds.)
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