By C.B. Anfinsen, M.L. Anson, John T. Edsall, Frederic M. Richards (Eds.)
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Extra resources for Advances in Protein Chemistry, Vol. 20
1957). Rev. 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).
Lower series: sedimentation of prcripitate without added ATP. From BettexGalland and Liischer (1961). precipitate wiIl form which sediments much faster than the voluminous product obtained in the absence of ATP. Grette (1963) has published such pictures of porcine thrombosthenin. The speed of the contraction of a superprecipitate is greatly dependent upon temperature. For thrombostheniii a t room temperature (about 20°C) 15 to 20 min are required for complete contraction. At 37°C this process requires only 1 to 2 min.
The same conditions were encountered with the contractile protein from human platelets (Bettex-Galland and von Tavel, unpublished observations, 1963). 7. The “Relaxing Factor” of the Blood Platelets-a of Thrombosthenin Activities Natural Inhibitor Recently, Grette (1963) has reported the extraction from pig platelets of a material with properties comparable to the “relaxing factor” from muscle (Marsh, l’~51). Solutions of this factor will inhibit superprecipitation as well as ATPase activity of thrombosthenin of porcine origin.
Advances in Protein Chemistry, Vol. 20 by C.B. Anfinsen, M.L. Anson, John T. Edsall, Frederic M. Richards (Eds.)