Regeneration of the Filtrable Forms of Salmonella enteritidis in Media containing Blood Plasma (Fibrin Structure)

Nature ◽  
1955 ◽  
Vol 176 (4474) ◽  
pp. 208-209 ◽  
Author(s):  
I. JUHÁSZ ◽  
J. VADÁSZ
Keyword(s):  
Blood Plasma ◽  
Salmonella Enteritidis ◽  
Fibrin Structure

scholarly journals Molting in Salmonella Enteritidis-Challenged Laying Hens Fed Alfalfa Crumbles. III. Blood Plasma Metabolite Response

2007 ◽  
Vol 86 (12) ◽  
pp. 2492-2501 ◽  
Author(s):  
C.S. Dunkley ◽  
J.L. McReynolds ◽  
K.D. Dunkley ◽  
L.F. Kubena ◽  
D.J. Nisbet ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Salmonella Enteritidis ◽  
Laying Hens ◽  
Plasma Metabolite

Activation of isolated heterophils from chicks stimulated in vivo with salmonella enteritidis-immune lymphokines

1996 ◽  
Vol 54 ◽  
pp. 760-761
Author(s):  
R. B. Moyes ◽  
R. E. Droleskey ◽  
M. H. Kogut ◽  
J. R. DeLoach
Keyword(s):  
Lamina Propria ◽  
Intestinal Mucosa ◽  
Salmonella Enteritidis ◽  
Intestinal Tract ◽  
Polymorphonuclear Cells ◽  
Subclinical Infection ◽  
Egg Products ◽  
Immune Lymphokines ◽  
Organ Invasion

Salmonella enteritidis (SE) is of great concern to the poultry industry due to the organism's ability to penetrate the intestinal mucosa of the laying hen and subsequently colonize the ovaries and yolk membrane. The resultant subclinical infection can lead to SE infection of raw eggs and egg products. Interference with the ability of the organism to invade has been linked to the activation and recruitment of inflammatory polymorphonuclear cells, heterophils, to the lamina propria of the intestinal tract.Recently it has been established that heterophil activation and increased resistance to SE organ invasion can be accomplished by the administration of SE-immune lymphokines (SE-ILK) obtained from supernatants of concanavalin-A stimulated SE immune T lymphocytes from SE hyperimmunized hens. Invasion of SE into the lamina propria provides a secondary signal for directing activated heterophils to the site of SE invasion.

Sweet's syndrome associated with Salmonella enteritidis infection

1999 ◽  
Vol 24 (3) ◽  
pp. 239-240 ◽  
Author(s):  
Flórez ◽  
Sánchez-Aguilar ◽  
Rosón ◽  
Prieto ◽  
Van den Eyden ◽  
...  
Keyword(s):  
Salmonella Enteritidis ◽  
Sweet’S Syndrome ◽  
Sweet's Syndrome

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

Protection from Hg-Inactivation of Factor XIII by Mercaptalbumin

1970 ◽  
Vol 24 (03/04) ◽  
pp. 352-355 ◽  
Author(s):  
P Fantl
Keyword(s):  
Blood Plasma ◽  
Factor Xiii ◽  
Active Component ◽  
Plasma Albumin ◽  
Plasma Factor ◽  
Mercuric Ions

SummaryThe blood plasma factor XIII (fibrin stabilizing factor) is inactivated by mercuric ions and can be reactivated by serum - or plasma albumin of which the active component is mercaptalbumin. A relation between mercaptalbumin concentration and factor XIII activity is pointed out.

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