Advances in Protein Chemistry, Vol. 20 by C.B. Anfinsen, M.L. Anson, John T. Edsall, Frederic M.

By C.B. Anfinsen, M.L. Anson, John T. Edsall, Frederic M. Richards (Eds.)

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Taking into consideration that thrombosthenin is present in ten times higher concentration than the contractile proteins in undifferentiated cells, such as those described by Hoffmann-Berling (1956), it is not astonishing that, in the latter case also, no evidence for any such structures has been detected. This of course leads to the questions as to the state in which these last mentioned proteins, as well as thrornbosthenin, are present within the cell. Let us recall that thrombosthenin is distinctly more soluble than muscle actomyosin, although it is still insoluble within the so-called physiological range of ionic strength.

1878). Arch. Physiol. Norm. 5, 692. Heilbrunn, L. V. (1961). In “The Functions of the Blood” (R. G. Macfarlane and A. H. T. ), p. 283. Blackwell, Oxford. Hellem, A. J. (1960). Scand. J . Lab. Clin. Invest. 12, Suppl. Hoffmann-Berlmg, H. (1954). Biochim. Biophys. Acta 14, 182. Hoffmann-Berling, H. (1956). Biochim. Biophys. Acta 19, 453. Hoffmann-Berling, H. (1960). I n “Comparative Biochemistry” (M. Florkin and H. S. ), Vol. 11, p. 341. Academic Press, New York. Hoffmann-Berling, H. (1961). Ergeb.

Contraction and elongation of this structure is then explained in terms of the more or less pronounced interdigitation of the actin and myosin moieties. This implies that even exteiisive contraction of the muscle is possible without a corresponding shortening of the myosin or actin fibers, respectively. On a molecular level the actin strands slide along the myosin chains (Huxley and Niedergerke, 1954; Huxley and Hanson, 1954; Huxley, 1963). This process must be due to the cyclic formation and breaking of weak bonds between the two constituents of the contractile complex.

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