Inhibitory effect of ginsenoside on the mediator release in the guinea pig lung mast cells activated by specific antigen-antibody reactions

1998 ◽  
Vol 20 (11) ◽  
pp. 625-641 ◽  
Author(s):  
J.Y. Ro ◽  
Y.S. Ahn ◽  
K.H. Kim
1980 ◽  
Vol 35 (9-10) ◽  
pp. 712-716 ◽  
Author(s):  
Joseph Veser ◽  
Helmut Thomas

Abstract Immunization of rabbits with purified catechol methyltransferase from Candida tropicalis yielded a potent antiserum. Ouchterlony double diffusion analysis showed a single precipitin line. There was no cross reactivity with the catechol methyltransferase from rat and bovine liver. Specific antigen-antibody interaction was demonstrated by a potent inhibitory effect of the antibody on the yeast enzyme. Immunological titration and quantitative precipitin reaction of the enzyme showed that the maximum amount of precipitable complex occurred at the equivalence point where enzyme activity was completely inhibited.


2003 ◽  
Vol 52 (0) ◽  
pp. s7-s8 ◽  
Author(s):  
A. Vannacci ◽  
M. B. Passani ◽  
S. Pierpaoli ◽  
L. Giannini ◽  
P. F. Mannaioni ◽  
...  

1953 ◽  
Vol 98 (4) ◽  
pp. 291-303 ◽  
Author(s):  
Georges Ungar ◽  
Evelyn Damgaard ◽  
Fred P. Hummel

The activation of profibrinolysin in sensitized guinea pig serum when mixed in vitro with the homologous antigen was confirmed with a more accurate and more reliable method than the one previously used. A study was made of some of the conditions required for obtaining maximum activation. Profibrinolysin activation was also induced in normal guinea pig serum by addition of certain "anaphylactoid" agents such as peptone, tween 20, morphine, octylamine, octadecylamine, and 48/80. The specific antigen and the anaphylactoid agents produce activation only when added to whole, fresh, unheated serum. Profibrinolysin activation by these agents, as opposed to activation by streptokinase, seems to require the intervention of a kinase system (serofibrinokinase) inactivated by fractionation of serum and by heating to 56°C. Whenever serum was submitted to treatments which caused fractionation, fixation or inhibition of complement, serofibrinokinase was also inactivated. Under the conditions investigated the behavior of this kinase was indistinguishable from that of complement.


1968 ◽  
Vol 51 (5) ◽  
pp. 677-693 ◽  
Author(s):  
F. Alonso-deFlorida ◽  
J. del Castillo ◽  
Xaviera García ◽  
E. Gijón

The mechanism of the contractions elicited by specific antigens in immunologically sensitized muscle tissue (Schultz-Dale responses) has been investigated on single fibers of denervated guinea pig hemidiaphragms. This preparation can be either actively or passively allergized, showing Schultz-Dale responses similar to those of visceral muscle. Specific antigens were applied with an electrically operated microtap to discrete areas of the cell surface while recording the electrical activity with intracellular microelectrodes. In this manner, a depolarizing action of the antigens on the muscle membrane was demonstrated. Brief applications of antigen gave rise to phasic potential changes (antigen potentials) similar to those elicited in the same fibers with acetylcholine-filled microtaps. However, antigen potentials occur only in denervated fibers sensitized to the specific antigen or closely related proteins; they are not seen in either innervated fibers of allergized animals or in denervated, nonallergized fibers. Repeated antigen application to the same area of the fiber causes a local irreversible desensitization. The antigen potentials are associated with a reduction in the resistance of the muscle membrane, similar to that caused by acetylcholine. It is concluded that besides causing the liberation of biogenic amines from the mast cells, antigens exert a direct action on the permeability of the muscle membrane; the molecules of antibody adsorbed to the cells appear to act as specific chemoreceptors for the antigen.


2005 ◽  
Vol 68 (23-24) ◽  
pp. 2063-2080 ◽  
Author(s):  
Ji Young Kim ◽  
Eun Young Kwon ◽  
Yun Song Lee ◽  
Won Bae Kim ◽  
Jai Youl Ro

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