Guinea Pig Serum in Relation to Prezone and Non-Specific Wassermann Reactions

1939 ◽  
Vol 9 (2) ◽  
pp. 136-150 ◽  
Author(s):  
John A. Kolmer
Keyword(s):  
1963 ◽  
Vol 10 (01) ◽  
pp. 120-132 ◽  
Author(s):  
E. S Olesen

SummaryTreatment of serum with bentonite led to a reduced content of inhibitors of trypsin and urokinase in the isoelectrically precipitated euglobulin, and removed fibrinolytic agents and precursors from serum. Bentonite-treated serum added to untreated serum reduced precipitation of the above inhibitors, and presumably also precipitation of inhibitors against a plasminogen activator of serum.Bentonite-treated serum (whether from pig, ox, guinea-pig, or man), added to untreated guinea-pig serum, produced fibrinolytic activity on isoelectric precipitation of the mixture; the activity of the euglobulin was due to an activator of plasminogen as well as an active protease, probably plasmin. The described effects of bentonite-treated serum are similar to those previously reported for anionic polyelectrolytes. Possible mechanisms are discussed.The “non-specific” activation of fibrinolytic activity by means of bentonite emphasizes that guinea-pig serum [which is characterized by a high potential for “nonspecific” activation of its fibrinolytic system Olesen (1962)] contains all the elements required for the formation of an activator of plasminogen, and thus the activation of its plasminogen to plasmin.


1975 ◽  
Vol 142 (5) ◽  
pp. 1065-1077 ◽  
Author(s):  
A.P. Osmand ◽  
R.F. Mortensen ◽  
Joan Siegel ◽  
H. Gewurz

Interactions of CRP with various substrates in the presence of human serum have been shown to result in efficient activation of C components C1-C5. We now report the ability of CRP to initiate C-dependent hemolysis. For this purpose CRP was isolated by affinity chromatography using pneumococcal CPS and gel filtration; its purity was established by several criteria. Erythrocytes were coated with CPS (E-CPS) and passively sensitized with CRP. C-dependent lysis of these cells was observed upon the addition of suitably absorbed human serum, and the efficiency of hemolysis compared favorably with that initiated by rabbit IgG anti-CPS antibody. CRP also sensitized E-CPS for lysis by guinea pig C; partial lysis was seen when C4-deficient guinea pig serum was used, suggesting that CRP also shares with antibody the ability of CRP to fully activate the C system and provide further evidence for a role for CRP similar to that of antibody in the initiation and modulation of inflammatory reactions via the complete system.


1963 ◽  
Vol 4 (1) ◽  
pp. 64-84
Author(s):  
I. Koefoed Jensen
Keyword(s):  

1970 ◽  
Vol 245 (11) ◽  
pp. 2797-2801 ◽  
Author(s):  
Helga M. Suld ◽  
Peter A. Herbut
Keyword(s):  

1963 ◽  
Vol 118 (1) ◽  
pp. 99-120 ◽  
Author(s):  
J. D. Broome

A number of the properties of the L-asparaginase present in guinea pig serum have been examined and shown to be indistinguishable from those of the agent responsible for inhibiting cells of lymphoma 6C3HED in vivo. The patterns of instability of the enzyme to changes in temperature and pH were found to parallel closely those of the antilymphoma agent. L-Asparaginase activity was essentially absent from the serum of newborn guinea pigs and this failed to inhibit 6C3HED cells. On separating guinea pig serum proteins by salt precipitation, electrophoresis, and chromatography on DEAE cellulose, antilymphoma activity was found only in fractions which contained L-asparaginase.


2007 ◽  
Vol 26 (3) ◽  
pp. 207-223 ◽  
Author(s):  
Göknur Güler ◽  
Zerrin Türközer ◽  
Nesrin Seyhan

1960 ◽  
Vol 111 (1) ◽  
pp. 93-106 ◽  
Author(s):  
Paul G. Klein ◽  
Peter M. Burkholder

Evidence is presented to show that guinea pig complement fixed on sensitized sheep red cells acts as a specific agglutinogen. Agglutinating antibodies that react with cell-fixed complement can be produced by immunizing rabbits with a complex of stromata-amboceptor-complement or with guinea pig serum globulin. These agglutinins can be removed by precipitation with guinea pig serum. They are, therefore, distinct from immunoconglutinins.


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