scholarly journals QUANTITATIVE CHEMICAL STUDIES ON COMPLEMENT OR ALEXIN

1942 ◽  
Vol 75 (3) ◽  
pp. 285-295 ◽  
Author(s):  
Michael Heidelberger ◽  
Manfred Mayer
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Human Complement ◽  
Modified Method ◽  
Chemical Studies ◽  
Quantitative Chemical ◽  
Pig Serum

1. A modified method is given for the titration of human complement so that C'1 titers are measured, as in guinea pig serum, instead of the C'2 titers yielded by the usual titration. 2. The measurement of complement combining component or components in weight units, instead of relative terms, is carried out as in guinea pig serum and leads to similar values, 0.03 to 0.05 mg. of C' N per ml. of human serum. 3. Other similarities in human and guinea pig complements are noted and discussed.

scholarly journals QUANTITATIVE CHEMICAL STUDIES ON COMPLEMENT OR ALEXIN

1941 ◽  
Vol 74 (4) ◽  
pp. 359-367 ◽  
Author(s):  
Michael Heidelberger ◽  
M. Rocha e Silva ◽  
Manfred Mayer
Keyword(s):  
Guinea Pig ◽  
Quantitative Data ◽  
Chemical Studies ◽  
Component C ◽  
Quantitative Chemical ◽  
Pig Serum

1. Quantitative data are given on the effect of variations in the time of contact and the proportions of the reactants on the quantity of complement combining component nitrogen (C'1 N) found in active guinea pig serum. 2. C'1 N was the same when determined with precipitates containing excess antibody or excess antigen. 3. Finely divided specific precipitates took up the complement combining component (C'1) from subsequently added guinea pig serum almost as well as specific precipitates formed in the presence of complement.

scholarly journals Interactions of C-reactive protein with the complement system. III. Complement-dependent passive hemolysis initiated by CRP.

1975 ◽  
Vol 142 (5) ◽  
pp. 1065-1077 ◽  
Author(s):  
A.P. Osmand ◽  
R.F. Mortensen ◽  
Joan Siegel ◽  
H. Gewurz
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Complete System ◽  
Gel Filtration ◽  
C Reactive Protein ◽  
Inflammatory Reactions ◽  
Reactive Protein ◽  
Rabbit Igg ◽  
The Complement System ◽  
Pig Serum

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.

THE EFFECT OF FREE FATTY ACIDS ON RESIN UPTAKE OF TRI-IODOTHYRONINE FROM HUMAN, RAT, RABBIT AND GUINEA-PIG SERUM AND HUMAN SERUM ALBUMIN

1969 ◽  
Vol 45 (4) ◽  
pp. 489-493 ◽  
Author(s):  
P. W. NATHANIELSZ
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Free Fatty Acids ◽  
Human Serum ◽  
Rat Serum ◽  
Pig Serum

SUMMARY Recently changes in plasma free fatty acids have been suggested as a possible regulator of the levels of free thyroxine in the plasma. Oleic acid has been shown to displace tri-iodothyronine from human serum, human serum albumin, rat serum, rabbit serum and guinea-pig serum. The extent of the displacement, much greater from human serum albumin than from whole serum, suggests that free fatty acid does not affect the globulin binding site. It would also appear that, in the rat, all the binding sites are sensitive to free fatty acids and hence there is probably only albumin binding in this species. The results with rabbit and guinea-pig serum were intermediate to those with human and rat serum. A significant rise in resin uptake of tri-iodothyronine in vitro occurred with an increase of free fatty acid level of 0·5 m-equiv./l., well within the physiological range.

scholarly journals Humoral immunostimulation. IV. Role of complement.

1975 ◽  
Vol 141 (4) ◽  
pp. 736-752 ◽  
Author(s):  
W T Shearer ◽  
J P Atkinson ◽  
M M Frank ◽  
C W Parker
Keyword(s):  
Cell Growth ◽  
Guinea Pig ◽  
Human Serum ◽  
Calf Serum ◽  
Rabbit Serum ◽  
Mouse Serum ◽  
Low Concentrations ◽  
High Concentrations ◽  
Nucleoside Uptake ◽  
Pig Serum

When L cells were treated with anti-L-cell antibody in medium containing heat-inactivated fetal calf serum, nucleoside uptake and cell growth were stimulated. The response was markedly increased when fresh, unheated sera from calves, guinea pigs, humans, mice, or rabbits were also present. The factors in unheated serum responsible for the enhancement of immunostimulation were studied. Using low concentrations of sera deficient in various complement (C) components and low concentrations of antibody no augmentation of immunostimulation was seen with Clr-deficient human serum, C2-deficient human serum, C2,4-deficient human serum, C4-deficient guinea pig serum, C3-C9-depleted guinea pig serum (by administration of cobra venom factor to animals), but stimulation was observed with C5-deficient human serum, C5-deficient mouse serum, and C6-deficient rabbit serum. When the concentration of anti-serum was raised, however, augmentation was observed with C4-deficient guinea pig serum. Thus, at low concentrations of antiserum enhancement appeared to occur through the classical C pathway, whereas at high concentrations of antibody either the classical or alternate C pathways appeared to be involved. Stimulation was specifically restored by purified C2 in C2-deficient serum and by C3 in C3-C9-deficient serum. Under the usual reaction conditions consumption of guinea pig C component C4 could be demonstrated which provided direct evidence for activation of the classical C pathway under conditions leading to immunostimulation. By immunofluorescence, cells treated with antibody and normal human serum had human C3 deposited at the cell surface. Taken together these observations suggest that C activated through C3 by either the classical or alternate pathways has the potential to enhance nucleoside incorporation into DNA and cell growth of cells exposed to limiting amounts of antibody. Although the mechanism of stimulation is unknown, it is likely to involve a direct effect of C3 at the level of the cell membrane.

Fibrinolytic system of guinea pig serum

1959 ◽  
Vol 196 (4) ◽  
pp. 775-778 ◽  
Author(s):  
Zbigniew Latallo ◽  
Stefan Niewiarowski ◽  
Alfred L. Copley
Keyword(s):  
Acetic Acid ◽  
Guinea Pig ◽  
Human Serum ◽  
Comparative Studies ◽  
Fibrinolytic Activity ◽  
Fibrinolytic System ◽  
Proteolytic Activities ◽  
Human Plasminogen ◽  
No Activation ◽  
Pig Serum

Comparative studies on 10 mammals showed that, in contrast to all the others, guinea pig serum alone, on precipitation with acetic acid, pH 5.3–5.4 at 4°C, yielded a euglobulin with high spontaneous fibrinolytic activity. Fibrinolytic and proteolytic activities of guinea pig, bovine and human euglobulins after addition of streptokinase (SK), SK-human plasminogen mixture, and without any activators were compared; antiplasmin activity was also investigated. When guinea pig serum was substituted for human serum in a mixture of the latter with SK, there was no activation of bovine plasminogen. A plasmin-antiplasmin complex may be the chief component of the guinea pig serum fibrinolytic system.

scholarly journals Chronic Hemolytic Anemia with Erythrocyte Fragility to Cold and Acid

Blood ◽  
1951 ◽  
Vol 6 (2) ◽  
pp. 124-141
Author(s):  
S. H. LIU
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Hemolytic Anemia ◽  
Hemolytic Activity ◽  
Sodium Sulphate ◽  
Chronic Hemolytic Anemia ◽  
Erythrocyte Fragility ◽  
Normal Controls ◽  
Paroxysmal Cold Hemoglobinuria ◽  
Pig Serum

Abstract In 2 cases of chronic hemolytic anemia with erythrocyte fragility to cold and acid, although the abnormality resides in the red blood cells, serum, whether from the patients or from normal controls, is necessary for the hemolysis. Complement is most likely not responsible for the serum hemolytic activity, because the latter, while similar to complement in certain properties, may be completely dissociated from it. From human serum the euglobulin separated by CO2 and sodium sulphate and the pseudoglobulin I obtained by sodium sulphate precipitation possess hemolytic activity for the cells of the patient and not those of the control. The hemolytic activity of these globulin fractions is increased by chilling and by addition of acid. It is inhibited by serum pseudoglobulin II and albumin. Guinea pig serum aids human serum in its hemolytic activity on susceptible human cells. This augmenting effect of the guinea pig serum is not due to its complement content, nor due to its hetero-hemolysin for all human erythrocyte. In view of the data presented in this and the preceding papers, a new syndrome is suggested which can be clearly differentiated from paroxysmal cold hemoglobinuria and from paroxysmal nocturnal hemoglobinuria.

scholarly journals QUANTITATIVE CHEMICAL STUDIES ON HEMOLYSINS

1942 ◽  
Vol 25 (4) ◽  
pp. 523-531 ◽  
Author(s):  
Michael Heidelberger ◽  
Henry P. Treffers
Keyword(s):  
Guinea Pig ◽  
Chemical Studies ◽  
Quantitative Chemical

1. Total antibody in hemolysins may be estimated from the nitrogen added to sheep stromata suspensions. 2. The method is applied to a number of hemolysins and a correlation, valid to within 20 per cent, established between hemolytic titer and total antibody. 3. When stromata combine with antibody in the presence of guinea pig complement they may take up at least 80 per cent of their weight of complement combining component(s).

scholarly journals STUDIES OF THE PLASMIN SYSTEM

1957 ◽  
Vol 106 (3) ◽  
pp. 423-437 ◽  
Author(s):  
Philip S. Norman
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Assay Method ◽  
Pig Serum

A general assay method involving casein digestion is shown to be applicable for determination of several components of the plasmin system. Total plasminogen of human serum can be measured by use of sufficient streptokinase for instantaneous activation, accompanied by protection of the active plasmin with casein. Total plasminogen of guinea pig serum can be measured after complete activation with streptokinase in combination with human activator. The activator principle in whole human serum can be measured by its ability to activate guinea pig plasminogen.

An Improved Procedure for Measuring Neuraminidase Antibodies by Hemagglutination-Inhibition

1972 ◽  
Vol 27 (3) ◽  
pp. 241-245 ◽  
Author(s):  
Alan P. Kendal ◽  
Elva Minuse ◽  
Fred M. Davenport
Keyword(s):  
Guinea Pig ◽  
Enzyme Inhibition ◽  
Hemagglutination Inhibition ◽  
Egg White ◽  
Inhibition Activity ◽  
Recombinant Viruses ◽  
Modified Method ◽  
Chicken Erythrocytes ◽  
Cell Variation ◽  
Pig Serum

Neuraminidase antibodies are known to inhibit hemagglutination by X-15 and X-15 (HK) recombinant viruses. However, the level of inhibition observed varies when different batches of chicken erythrocytes are employed, and the test generally detects neuraminidase antibodies with less sensitivity than an enzyme inhibition test. By titrating neuraminidase antibodies in the presence of anti-IgG globulins, with appropriate specificity, the hemagglutination-inhibition activity of neuraminidase antibodies is enhanced and the effect of cell variation is minimized. Consequently results obtained with this modified method for titrating neuraminidase antibodies become comparable to those obtained by measuring enzyme-inhibition. The improved hemagglutination-inhibition procedure possesses the important advantages of greater convenience and economy. Similar enhancing effects may also be obtained with egg white and guinea pig serum.

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