The Use of Complement Fixation Tests to Detect Australia Antigen-Antibody Complexes and Antibodies to a Tween Antigen

Vox Sanguinis ◽  
1973 ◽  
Vol 24 (1) ◽  
pp. 36-43
Author(s):  
L. Thiry ◽  
G. Client ◽  
C. Toussaint ◽  
P. Vereerstraeten
Keyword(s):  
Complement Fixation ◽  
Australia Antigen ◽  
Antigen Antibody

Rapid detection of Australia/SH antigen and antibody by a simple and sensitive technique of immunoelectronmicroscopy

1971 ◽  
Vol 17 (7) ◽  
pp. 993-1000 ◽  
Author(s):  
A. E. Kelen ◽  
A. E. Hathaway ◽  
D. A. McLeod
Keyword(s):  
Complement Fixation Test ◽  
Complement Fixation ◽  
Practical Method ◽  
Rapid Screening ◽  
Blood Products ◽  
Agar Gel ◽  
Virus Particles ◽  
Antigen Antibody ◽  
Filtration Technique ◽  
Electronmicroscopic Examination

A simple and practical method is presented for demonstrating the presence of the Australia/SH antigen and its corresponding antibody in serum specimens, both qualitatively and quantitatively. The method is based on the electronmicroscopic visualization of characteristic aggregates of antigen–antibody complexes formed in the mixture of a serum specimen and the appropriate Australia/SH detector reagent. It involves the use of a microtechnique requiring minute amounts of reagents and provides, as a result of diffusion and filtration through agar gel, partially purified and concentrated preparations, ready for electronmicroscopic examination in less than an hour. The method is highly specific and yields reproducible results. Its sensitivity was found to be greater than that of the crossover electrophoresis test and closely approximates that of the complement fixation test, with the added advantage of not being affected by the "prozone phenomenon." The method can be recommended for use in laboratories equipped with electronmicroscopic facilities to establish a differential diagnosis of viral hepatitis cases, perform rapid screening of blood samples (blood products) for the presence of Australia/SH antigen, and clarify equivocal results obtained by other methods. It is expected that the agar–diffusion–filtration technique will also prove useful, in general, for enhancing the chances of detecting virus particles in suspensions of relatively low virus concentrations.

Radioimmunoprecipitation Assay for Australia Antigen, Antibody, and Antigen-Antibody Complexes

1971 ◽  
Vol 138 (1) ◽  
pp. 249-257 ◽  
Author(s):  
J. A. Coller ◽  
I. Millman ◽  
T. C. Halbherr ◽  
B. S. Blumberg
Keyword(s):  
Australia Antigen ◽  
Radioimmunoprecipitation Assay ◽  
Antigen Antibody

scholarly journals THE INACTIVATION OF COMPLEMENT AND ITS COMPONENTS BY PLASMIN

1953 ◽  
Vol 97 (4) ◽  
pp. 573-589 ◽  
Author(s):  
Louis Pillemer ◽  
Oscar D. Ratnoff ◽  
Livia Blum ◽  
I. H. Lepow
Keyword(s):  
Human Serum ◽  
Proteolytic Enzyme ◽  
Complement Fixation ◽  
Hydrogen Ion ◽  
Complement Components ◽  
High Hydrogen ◽  
Ion Concentrations ◽  
Plasmin Inhibitors ◽  
Antigen Antibody

Human complement is inactivated by plasmin, the proteolytic enzyme of plasma or serum active at or near neutrality. The addition of streptokinase to human serum, which converts plasminogen to plasmin, also causes the inactivation of complement components C'2 and C'4 and varying amounts of C'1. C'3 is the most resistant to inactivation by plasmin. Chloroform-activated human plasmin and bovine plasmin also destroy these components of complement, but are less effective than the streptokinase-activated enzyme. The inactivation of complement by the addition of streptokinase to human serum is inhibited by high hydrogen ion concentrations, low temperature, and elevated ionic strength. The inactivation of the components of complement in various fractions of serum is influenced by the available plasminogen and the content of plasmin inhibitors in these fractions. Certain similarities are pointed out between the components of complement and the factors in the plasmin system and between the inactivation of the components of complement by antigen-antibody reactions, by specific agents, and by plasmin. The possible significance of these relationships in immune hemolysis and complement fixation, and the possible role of the plasmin system in the instability of complement and the development of anticomplementary properties in serum are discussed.

Independence of activation of the fibrinolytic system from certain immunologic systems

1959 ◽  
Vol 196 (2) ◽  
pp. 431-435 ◽  
Author(s):  
S. N. Kolmen ◽  
D. R. Celander ◽  
M. Mason Guest
Keyword(s):  
Fibrinolytic Activity ◽  
Complement Fixation ◽  
Fibrinolytic System ◽  
Complement Activity ◽  
Antibody Reaction ◽  
Antigen Antibody

Activation of the immunologic system either in vitro or in vivo results in nearly complete consumption of complement without activation of the fibrinolytic system. However complement activity decreased upon the induction of fibrinolytic activity even in the absence of an antigen-antibody reaction. Presumably this is due to proteolysis of some part of the complement complex since complement activity was found to be destroyed in the presence of small quantities of purified fibrinolysin. These observations are consistent with the conclusion that a) the components of complement and those of the fibrinolytic system are separate and discrete entities; b) that reactions involving complement fixation and activation do not directly influence the fibrinolytic system; and c) that activation of the fibrinolytic system results in decreases in complement through proteolysis of one or more of its components by the fibrinolysin which develops.

scholarly journals SPECIFIC FRACTIONATION OF HUMAN ANTIDEXTRAN ANTIBODIES

1964 ◽  
Vol 119 (6) ◽  
pp. 983-995 ◽  
Author(s):  
Justus Gelzer ◽  
Elvin A. Kabat
Keyword(s):  
Molecular Weight ◽  
Complement Fixation ◽  
Microcomplement Fixation ◽  
Antigen Antibody ◽  
Two Populations ◽  
Good Agreement

Human antidextran of one individual, absorbed specifically on sephadex, was fractionated into two populations of antibody molecules by successive elution with oligosaccharides of the isomaltose series of increasing size. The purified antibody fractions and some whole antidextran sera were found to fix complement with dextrans of molecular weight of 195,000 and above. It could be demonstrated by quantitative microcomplement fixation inhibition assays that the antibody eluted with isomaltotriose had a higher affinity for smaller oligosaccharides relative to isomaltohexaose, indicating a high content of antibody molecules with smaller combining sites, while with the second fraction, eluted with isomaltohexaose, the small haptens were very poor inhibitors and the larger oligosaccharides inhibited readily, presumably due to a higher proportion of molecules with larger combining site size. Assays of similarly prepared fractions, obtained from earlier bleedings of the same individual (1), with inhibition of complement fixation were in good agreement with those obtained by inhibition of precipitation. The two purified antidextran fractions were shown to differ with respect to their complement-fixing capacity. The fraction with molecules with smaller size-combining sites fixed only about half as much complement per unit antibody N as did the fraction containing largely molecules with larger combining sites suggesting that the strength of complement fixation is affected by the strength of the antigen-antibody interaction.

Nonenzymic glycation of human immunoglobulins does not impair their immunoreactivity.

1989 ◽  
Vol 35 (6) ◽  
pp. 1039-1042 ◽  
Author(s):  
L G Morin ◽  
G E Austin ◽  
G E Rodey ◽  
J E Johnson
Keyword(s):  
Complement Fixation ◽  
Diabetic Patients ◽  
Cell Agglutination ◽  
Varicella Zoster ◽  
Susceptibility To Infection ◽  
Human Immunoglobulins ◽  
Functionally Impaired ◽  
Antigen Antibody ◽  
Binding Cell ◽  
Increased Susceptibility

Abstract Diabetic patients have an increased proportion of their immunoglobulins nonenzymically glycated. To investigate the possibility that this may contribute to increased susceptibility to infection, we compared the immunoreactivity of glycated and nonglycated human immunoglobulins against rubella and hepatitis; streptococcal exoenzyme and infectious mononucleosis; human lymphocytotoxic antigens (HLA); and Varicella zoster in terms of antigen-antibody binding, cell agglutination, cytotoxicity, and complement-fixation properties, respectively. We found no evidence to support the supposition that glycated immunoglobulins are functionally impaired.

scholarly journals SEROLOGICAL STUDIES IN RHEUMATIC FEVER

1949 ◽  
Vol 89 (6) ◽  
pp. 669-680 ◽  
Author(s):  
Edward E. Fischel ◽  
Ruth H. Pauli
Keyword(s):  
Rheumatic Fever ◽  
Complement Fixation ◽  
Specific Antigen ◽  
Phase Reaction ◽  
Tissue Extracts ◽  
Serological Studies ◽  
Specific Antigens ◽  
Wassermann Reaction ◽  
Antigen Antibody ◽  
And Control

1. An attempt was made to repeat and extend various tests which have been presumed to demonstrate specific antigens and antibodies in rheumatic fever. 2. The "phase reaction" appears to be an inconstant phenomenon probably related to a colloidal abnormality of the serum, rather than to a specific antigen-antibody system. 3. No specific autoantibodies to human tissue extracts were demonstrable by complement fixation or by the collodion particle technique. Variable results were noted with the same test sera on different occasions, and positive reactions with control tissues and control sera were observed. 4. The possibility should be considered that autoantibodies are not necessarily specific for rheumatic fever but may be manifestations of the occurrence of a type of reaction similar to a biologically false positive Wassermann reaction.

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