Advances in Protein Chemistry, Vol. 20 - download pdf or read online

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

Show description

Read Online or Download Advances in Protein Chemistry, Vol. 20 PDF

Best nonfiction_2 books

Merlin: A Casebook (Arthurian Characters and Themes, 10) by Peter Goodrich PDF

This e-book bargains with all points of the Merlin legend, from its origins to its expression in medieval and glossy literature, movie, and pop culture. Following a longer creation and an entire bibliography, the quantity bargains approximately twenty essays-some newly commissioned for this quantity others chosen from an important scholarly and important experiences of Merlin and his position.

Read e-book online The Cowslip Or More Cautionary Stories In Verse (1811) PDF

This ebook is a facsimile reprint and should comprise imperfections comparable to marks, notations, marginalia and mistaken pages.

Read e-book online Mechanosensitivity and Mechanotransduction PDF

This publication provides the most recent findings within the box of study of mechanosensitivity and mechanotransduction in numerous cells and tissues. Mechanosensitivity and mechanotransduction of the center and vascular cells, within the lung, in bone and joint tissues, in sensor platforms and in blood cells are defined intimately.

Additional info for Advances in Protein Chemistry, Vol. 20

Sample text

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.

Download PDF sample

Rated 4.35 of 5 – based on 33 votes

Related posts