Mathematical aspects of kinetic model equations for binary gas mixtures

1975 ◽  
Vol 16 (4) ◽  
pp. 776-782 ◽  
Author(s):  
David E. Greene
1964 ◽  
Vol 7 (12) ◽  
pp. 2012 ◽  
Author(s):  
T. F. Morse

AIAA Journal ◽  
1996 ◽  
Vol 34 (10) ◽  
pp. 2071-2081 ◽  
Author(s):  
J. Y. Yang ◽  
J. C. Huang ◽  
C. S. Wang

1965 ◽  
Vol 8 (3) ◽  
pp. 418 ◽  
Author(s):  
Bernard B. Hamel
Keyword(s):  

1973 ◽  
Vol 10 (3) ◽  
pp. 425-431
Author(s):  
Ta-Ming Fang

A previously developed set of kinetic model equations for a chemically-reacting gas is modified. By examining closely the H theorem, a new set of constraints is obtained. These conditions are then used to determine the inelastic collision parameters proposed in the model. The kinetic equations so obtained are able to produce exactly the same rate equations as prescribed by the actual chemical reactions.


Author(s):  
Maria A. Rydalevskaya ◽  
Yulia N. Voroshilova

Model kinetic equations are proposed for the description of ionized monoatomic gas mixture flows. The mixtures are assumed enough rarefied to be treated as ideal gases after multiple ionization steps. The model equations contain the equilibrium distribution functions for the components of the gas mixtures under consideration like it was done in BGK equations and their well-known generalizations. However, in this paper the new forms of the equilibrium distribution functions are used which correspond to the entropy maximum under the constraints of momentum, total energy, nuclei and electrons (both bound and free) conservation. It is shown that the derived model equations allow us to study the local equilibrium flows of the ionized gases and the transport processes of energy, nuclei and electrons in the non-equilibrium conditions.


1987 ◽  
Author(s):  
E B Reeve

A kinetic model, based on published studies of thrombin neutralization, is used to examine factors that limit spread of free thrombin in a simple plasma. It employs equations with presently available rate parameters which describe the courses of the major thrombin-binding reactions at 37°C in buffered saline solutions approximating plasma ultrafiltrate. Thrombin is bound reversibly by fibrinogen and fibrin-1 polymers as enzyme-substrate complexes (1) and by “fibrin” at a non-proteolyt ic site (2), and essentially irreversibly by antithrombins (3). These bindings reduce free thrombin levels and so limit spread of activity. The model equations with parameters from (1) and (3) show that thrombin neutralization by thrombin-substrate complexes is very brief and thrombin-antithrombin reactions are much too slow for early reduction of thrombin activity. However, parameters from (2) show that rapid reversible binding of thrombin by “fibrin” much reduces level of free thrombin and the level continues to fall as the thrombin is passed to the antithrombins. The model shows that a rapidly-acting antithrombin (e.g. heparin-ATIII) could reduce free thrombin fast enough to inhibit slower thrombin activations (e.g. of FXIII), and that a sufficient concentration of a reversible binder can govern the level of free thrombin. This suggests that a non-toxic reversible binder, with suitable Kd and half-life, would be valuable in treating thrombosis. Verification and extension of the model findings require better experimental definition of the parameters.(1) Lewis, S.D. et al. J. Biol. Chem. 260, 10192-10199, 1985.(2) Liu, C.Y. et al. J. Biol. Chem. 254, 10421-10425, 1979.(3) Jordan, R. et al. J. Biol. Chem. 254, 2902-2913, 1979. (Supported by grants from the Colorado Heart Foundation)


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