Download Human Blood Coagulation: Biochemistry, Clinical by H. C. Hemker M.D., E. A. Loeliger M.D., J. J. Veltkamp M.D. PDF

By H. C. Hemker M.D., E. A. Loeliger M.D., J. J. Veltkamp M.D. (auth.), H. C. Hemker M.D., E. A. Loeliger M.D., J. J. Veltkamp M.D. (eds.)

Since 1952, postgraduate classes for training physicians and speci­ alists were given by means of the scientific school of the collage of Leiden within the Boerhaave region, within which such a lot of its clinics and laboratories can be found. in the course of those years, contemporary advances in a large choice of m~dical fields and topics were mentioned via distin­ guished audio system from many nations. The gradually expanding atten­ dance has proven that, as should be anticipated from the swift growth of contemporary drugs, there's a greatly felt desire for this type of postgra­ duate research. In 1957, accordingly, the Leiden scientific college appointed an enduring committee for the association of postgraduate clinical schooling. Of the classes given when you consider that then, definite fabric proved to have adequate speedy clinical worth to justify e-book, and it now provides the Committee nice excitement to announce that during collaboration with the Leiden college Press it's going to post the Boerhaave sequence for Postgraduate scientific schooling. the 1st quantity of this new sequence is the made from the path on Human Blood Coagulation given in Novem­ ber 1968. it truly is our desire that this publication will turn out precious not just to people who participated within the direction but additionally to many others operating during this and linked fields.

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Additional info for Human Blood Coagulation: Biochemistry, Clinical Investigation and Therapy

Example text

The form of binding represented in figure 7A meets the requirements of the experimental data. However, the type of binding depicted in 7c, where the solvent around these residues is incorporated along with the protein into the lipid matrix, cannot be ruled out. However, even in 7A the contact of lipid with protein has been limited by the presence of this solvent. The conformational changes of prothrombin on being bound to the phospholipid cluster (as represented by figure 7D and E) are probably limited or absent.

Med. 23,569 (1963). , C. J. Hanahan, Biochem. Biophys. Acta. 90, 436 (1964). , C. R. Harmison, W. H. ]. Biochem. Physiol. 41, 2409 (1963). , M. Blomback, Nature 198,886 (1963). , S. P. Bessman, Blood II, 916 (1956). , D. H. Waugh, Thromb. Diathes. haemorrhag. 2,188 (1958). Tishkoff, G. , L. C. Williams, D. M. Brown,]. Bioi. Chem. 2443, 4151 (1968). , D. R. Kominz, P. Symonds, L. Lorand, W. H. Seegers, Arch. Biochem. , Arkiv Kemi 22,271 (1965). , Arkiv Kemi 23, 285 (1965). Seegers, W. , Prothrombin (1962).

A further attempt was made to determine more accurately the hydrated density of the complex through the use of a density gradient technique. In a linear 5-25% sucrose gradient, the complex sedimented to a point about one-third down the tube (figure 2). OI gjml. This corresponds to densities characteristic of Sf class 0-10 or low density f3-lipoprotein. ~ ~ 5 ~ \:; (;) .... ~ o o+---~--~--~~ o Bottom 2 3 Mill i liters 4 5 6 0 Top Fig. 2. Density gradient centrifugation of prothrombin activation mixture in a 5-25% sucrose gradient in the presence of calcium ions.

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