By C.B. Anfinsen, M.L. Anson, John T. Edsall, Frederic M. Richards (Eds.)
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Additional info for Advances in Protein Chemistry, Vol. 20
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. It should be kept in mind, however, that it might be possible that the ionic concentration is not constant throughout the different compartments of a cell. Furthermore, the ATP concentration is equally if not more important for the solubility of the contractile substances, and again, adequate methods for estimating local concentrations of the nucleotide in different regions of the cytoplasm are not yet available.
Hematol. 12, 16. Bounameaux, Y. (1959). Compt. Rend. SOC. Biol. 153, 865. Bounameaux, Y. (1961). Thromb. Diath. Haemorrhag. 6, 504. , and Sailer, S. (1960). Acta Haematol. 24, 311. Briggs, F. , and Fuchs, F. (1960). Biochim. Biophys. Acta 42, 519. Budtz-Olsen, 0. E. (1951). ” Blackwell, Oxford. , Edwards, G. , and Ruska, H. (1957). J . Biophys. Biochem. Cytol. 3, 867. Castaldi, P. , Firkin, B. , Blackwell, P. , and Clifford, K. J. (1962). Blood 20, 566. Chen, T. , and Tsai, L. (1948). J . Physiol.
Details see Bettex-Galland et al. (1962). For seems the more remarkable because the thrombosthenin components are of human origin. Of particular interest were the ATPase activities of the fragments and of the recombined complexes. Thrombosthenin M is a considerably weaker ATPase than thrombosthenin. Thrombosthenin A, as mentioned before, is completely inactive, but it is capable of potentiating the enzymatic 20 M. BEWEX-GALLAND AND E. F. LUSCHER activity of thrombosthenin M. Here again, it was found that actin from rabbit muscle exerts the same enhancing effect toward the thrombosthenin M ATPase.