A New Design Strategy for Molecular Recognition in Heterogeneous Systems:  A Universal Crystal-Face Growth Inhibitor for Barium Sulfate

AbstractRapid development of community health information networks raises the issue of semantic interoperability between distributed and heterogeneous systems. Indeed, operational health information systems originate from heterogeneous teams of independent developers and have to cooperate in order to exchange data and services. A good cooperation is based on a good understanding of the messages exchanged between the systems. The main issue of semantic interoperability is to ensure that the exchange is not only possible but also meaningful. The main objective of this paper is to analyze semantic interoperability from a software engineering point of view. It describes the principles for the design of a semantic mediator (SM) in the framework of a distributed object manager (DOM). The mediator is itself a component that should allow the exchange of messages independently of languages and platforms. The functional architecture of such a SM is detailed. These principles have been partly applied in the context of the HEllOS object-oriented software engineering environment. The resulting service components are presented with their current state of achievement.

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Investigations on the Nature of Hemophilia A

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654959 ◽

1963 ◽

Vol 09 (01) ◽

pp. 030-052 ◽

Cited By ~ 4

Author(s):

Eberhard Mammen

Keyword(s):

Factor Viii ◽

Human Plasma ◽

Barium Sulfate ◽

Freeze Drying ◽

Room Temperature ◽

Hemophilia A ◽

Normal Human Plasma ◽

Normal Human ◽

And Storage ◽

Prothrombin Activation

SummaryIn this paper an inhibitor is described that is found in hemophilic plasma and serum different from any till now described inhibitor. The inhibitor only inhibits prothrombin activation in the “intrinsic clotting systems”. This inhibitor is probably not present in normal human plasma or serum. It is destroyed by ether and freeze drying, is labile to acid and storage at room temperature. It is stable upon dialysis and has not been adsorbed on barium sulfate, aluminum hydroxide or kaolin. It precipitates at 50% v/v saturation with alcohol. The nature of this inhibitor seems to be a protein or lipoprotein.Factor VIII was isolated from hemophilic plasma. The amount isolated was the same as from normal plasma and the activity properties were not different. Hemophiliacs have normal amounts of factor VIII.

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“In vitro” Neutralization with Oxalate Ion of the Anticoagulant Effect of Heparin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654928 ◽

1961 ◽

Vol 05 (02) ◽

pp. 314-318 ◽

Cited By ~ 1

Author(s):

W. O Cruz ◽

L Meis ◽

C. P Dietrich

Keyword(s):

Calcium Oxalate ◽

Aluminium Hydroxide ◽

Barium Sulfate ◽

Anticoagulant Effect ◽

Normal Plasma ◽

Oxalate Ion

SummaryHeparinized blood or plasma coagulates if, after addition of oxalate, recalcification follows. Of the decalcifying agents only oxalate ion has been suitable for demonstrating this phenomenon. Oxalate seem to accomplish two different roles connected with this effect: a fundamental one, i. e., to sensitize a heparinlipoprotein complex to the action of an anti-heparin factor found in normal plasma or serum and a secondary one, related to its capacity to adsorb this antiheparin factor. The latter is removable by centrifugation. This anti-heparin oxalate factor, which is able to counteract the action of heparin after previous addition of oxalate, was found in sequestrened, Dowex 50 resin plasma or in serum, but is not active in citrated plasma. This factor was removed from plasma by adsorption with barium sulfate, aluminium hydroxide or calcium oxalate and was eluted from these adsorbants after incubation with saline.

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