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 through the scientific college of the college of Leiden within the Boerhaave area, within which such a lot of its clinics and laboratories can be found. in the course of those years, fresh advances in a large choice of m~dical fields and matters were mentioned via distin­ guished audio system from many nations. The progressively expanding atten­ dance has proven that, as should be anticipated from the speedy growth of contemporary medication, there's a greatly felt desire for this way of postgra­ duate research. In 1957, accordingly, the Leiden scientific school appointed an everlasting committee for the association of postgraduate scientific schooling. Of the classes given considering then, convinced fabric proved to have enough instant medical worth to justify booklet, and it now provides the Committee nice excitement to announce that during collaboration with the Leiden collage Press it's going to submit the Boerhaave sequence for Postgraduate scientific schooling. the 1st quantity of this new sequence is the made of the direction on Human Blood Coagulation given in Novem­ ber 1968. it truly is our wish that this booklet will end up worthy not just to people who participated within the path but in addition to many others operating during this and linked fields.

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

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DISCUSSION E. Hogenauer: Preliminary investigatons on the protein chemistry of factors vn and x. The impressive results presented by Dr. Magnusson in-dicate that the time is ripe for the application of methods used in molecular biology to solve problems of blood coagulation. Our group has been engaged in the purification and chemical characterization of the blood-clotting factors VII and x. We felt that this could contribute to the resolution of the unsettled controversy as to whether prothrombin is the common precursor of both these factors.

The prothrombin complex is also converted slowly to thrombin on standing with the synthetic polycations poly L-Iysine, poly L-ornithine, and protamine (3 2 ). The N-terminal amino acid of bovine prothrombin complex and NATURE OF PROTHROMBINASE 43 prothromin is alanine (28, 33). 7; small amounts of phenylalanine, aspartic acid, and threonine were also found. Biological activation yielded essentially the same N-terminal amino acids, except that 1 mole of N-terminal threonine was found. The yield of N-terminal amino acids was depressed by the addition of DFP (28).

Mixtures of factor 1Xa, thrombin, calcium chloride, and different levels of factor VIII were incubated. In a the curves show the disappearance offactor VIII with time, and in b the curves show the appearance offactor x activator, c and d are theoretical curves. Fig. 48 INTERACTION OF FACTORS VII, IX AND X 49 that factor VIII was a substrate in this reaction, and that formation of the factor X activator was catalysed by both activatedfactor IX (factor Ixa) and thrombin. The effect of thrombin was unmistakebly clearcut.

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