The Suppression of Antibody Production to Serum Protein Antigens in Guinea-Pigs

1966 ◽  
Vol 29 (3) ◽  
pp. 254-263 ◽  
Author(s):  
W.O. Weigle
Keyword(s):  
Serum Protein ◽  
Antibody Production ◽  
Guinea Pigs ◽  
Protein Antigens ◽  
Suppression Of Antibody Production

PARALLEL STUDIES OF COMPLEMENT AND COAGULATION IV. EFFECT OF CARBON TETRACHLORIDE

1951 ◽  
Vol 29 (2) ◽  
pp. 48-58
Author(s):  
Christine E. Rice ◽  
Paul Boulanger ◽  
P. J. G. Plummer
Keyword(s):  
Carbon Tetrachloride ◽  
Liver Injury ◽  
Serum Protein ◽  
Guinea Pigs ◽  
Fatty Degeneration ◽  
Blood Groups ◽  
Total Serum Protein ◽  
Total Serum ◽  
Coagulation Time ◽  
Complement Activity

To determine whether liver injury would result in a parallel decline in the complement titer and coagulative properties of the blood, groups of guinea pigs were given series of injections of the liver poison, carbon tetrachloride. Marked fatty degeneration of the liver, a decline in total serum protein and albumin, a decrease in complement activity, and a prolongation of coagulation time was observed in the treated animals. A general relationship was noted between the albumin-globulin ratio and the complement titer of the serum and between the complement titer and the coagulation time of the plasma.

T cell-dependent suppression of antibody production. I. Characteristics of suppressor T cells following tolerance induction

1978 ◽  
Vol 8 (5) ◽  
pp. 360-370 ◽  
Author(s):  
A. Basten ◽  
J. F. A. P. Miller ◽  
R. Loblay ◽  
P. Johnson ◽  
Jennifer Gamble ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Antibody Production ◽  
Tolerance Induction ◽  
Suppressor T Cells ◽  
Suppression Of Antibody Production

scholarly journals Restorative effect of traxanox on the suppression of antibody production in BALB/c mice.

1986 ◽  
Vol 87 (1) ◽  
pp. 19-28
Author(s):  
Masao HISADOME ◽  
Kazuhiro GOTO ◽  
Yukinobu KADOBE ◽  
Chiyuki ABE ◽  
Yuichi SHIOKAWA
Keyword(s):  
Antibody Production ◽  
Suppression Of Antibody Production

Serum protein fractions in bacteria-free guinea pigs investigated by disc electrophoresis

1969 ◽  
Vol 68 (5) ◽  
pp. 1235-1237
Author(s):  
O. V. Chakhava ◽  
V. A. Chibisova ◽  
K. L. Shakhanina ◽  
T. I. Tsatsenkina
Keyword(s):  
Serum Protein ◽  
Guinea Pigs ◽  
Disc Electrophoresis ◽  
Protein Fractions

scholarly journals Spatial requirements between haptenic and carrier determinants for T-dependent antibody responses.

1978 ◽  
Vol 148 (3) ◽  
pp. 817-822 ◽  
Author(s):  
S Fong ◽  
D E Nitecki ◽  
R M Cook ◽  
J W Goodman
Keyword(s):  
B Cells ◽  
Antibody Production ◽  
Guinea Pigs ◽  
Effective Interaction ◽  
Antibody Responses ◽  
T And B Cells ◽  
Axial Translation ◽  
Bifunctional Compounds

To gauge the proximity between cooperating T and B cells required for effective triggering of antibody production, guinea pigs were immunized with bifunctional antigens in which the haptenic and carrier determinants were separated by rigid spacers of varied dimension. These took the form 2,4-dinitrophenol-(proline)n-L-tyrosine-p-azobenzenearsonate, where n varied from 1 to 40 proline residues. Animals immunized with n = 10 and n = 22 compounds made strong anti-DNP antibody responses, whereas animals immunized with bifunctional compounds containing longer spacers did not make antibody detectable by precipitation. It can be calculated on the basis of very strong physicochemical evidence for the rigidity and axial translation of poly-L-proline chains in solution that the cut-off point for effective interaction between T and B cells lies between 69 and 97 A U.

scholarly journals Lack of Protection in Mice and Necrotizing Bronchointerstitial Pneumonia with Bronchiolitis in Guinea Pigs Immunized with Vaccines Directed against the hsp60 Molecule ofMycobacterium tuberculosis

2000 ◽  
Vol 68 (6) ◽  
pp. 3674-3679 ◽  
Author(s):  
Oliver C. Turner ◽  
Alan D. Roberts ◽  
Anthony A. Frank ◽  
Susan W. Phalen ◽  
David M. McMurray ◽  
...  
Keyword(s):  
Heat Shock ◽  
Guinea Pigs ◽  
Lung Damage ◽  
Dna Encoding ◽  
Protein Antigens ◽  
Plasmid Vaccine ◽  
Potential Vaccine ◽  
Guinea Pig Model ◽  
Shock Proteins ◽  
Severe Lung

ABSTRACT In this study, the hsp60 and hsp70 heat shock protein antigens ofMycobacterium tuberculosis were tested as potential vaccine candidates, using purified recombinant protein antigens or antigens encoded in the form of a DNA plasmid vaccine. Guinea pigs vaccinated with a mixture of the two proteins showed no evidence of resistance to low-dose aerosol challenge infection and quickly developed severe lung damage characterized by necrotizing bronchointerstitial pneumonia and bronchiolitis. As a result, we turned instead to a DNA vaccination approach using a plasmid encoding the hsp60 antigen of M. tuberculosis. Although immunogenic in mice, vaccination with plasmid DNA encoding hsp60 was not protective in that model or in the guinea pig model and again gave rise to similar severe lung damage. This study seriously questions the safety of vaccines against tuberculosis that target highly conserved heat shock proteins.

STUDIES ON THE LIVETINS OF HEN'S EGG YOLK: I. IDENTIFICATION OF PAPER-ELECTROPHORETIC AND IMMUNOELECTRO-PHORETIC LIVETIN FRACTIONS WITH SERUM PROTEIN ANTIGENS BY IMMUNOELECTROPHORETIC ANALYSIS

1964 ◽  
Vol 42 (6) ◽  
pp. 871-881 ◽  
Author(s):  
Chi-Ching Mok ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Egg Yolk ◽  
Paper Electrophoresis ◽  
Protein Antigens ◽  
Immunoelectrophoretic Analysis ◽  
Hen’S Egg ◽  
Alpha Beta

Immunoelectrophoretic analysis of an egg yolk livetin preparation has demonstrated the presence of six distinct fractions, which were numbered 1, 2, 3, 4, 5, and 6 from the anodic end of the electropherogram. Four of these fractions have been identified with four livetin fractions obtained by paper electrophoresis as follows: immunoelectrophoretic fraction 1 with alpha-livetin, fraction 2 with beta-livetin, fraction 4 with gamma1-livetin, and fraction 5 with gamma2-livetin.Immunoelectrophoresis of hen serum or cock serum against antilivetin serum has shown that both hen and cock sera contain antigens electrophoretically and immunologically identical to alpha-, beta-, gamma1-, and gamma2-livetins.

scholarly journals THE IN VIVO FORMATION AND FATE OF ANTIGEN-ANTIBODY COMPLEXES FORMED BY FRAGMENTS AND POLYPEPTIDE CHAINS OF RABBIT γG-ANTIBODIES

1966 ◽  
Vol 123 (6) ◽  
pp. 999-1012 ◽  
Author(s):  
Hans L. Spiegelberg ◽  
William O. Weigle
Keyword(s):  
Guinea Pigs ◽  
Protein Antigens ◽  
Fc Fragment ◽  
Fab Fragments ◽  
Antigen Antibody ◽  
Polypeptide Chains ◽  
Specific Rabbit ◽  
Antibody Excess

The in vivo formation and subsequent fate of complexes formed between specific rabbit γG-antibody subunits and circulating protein antigens was studied in rabbits and guinea pigs. Subunits obtained from purified antibodies were injected immediately after an injection of antigen, and the elimination from the circulation of either I*-labeled γG-subunits or labeled antigen determined. In the absence of antigen, all γG-subunits which lack the Fc fragment were rapidly eliminated. In the presence of excess antigen, F (ab')2, Fab and Fd fragments reacted with antigen and remained in the circulation as complexes which were eliminated at the same rate as the antigen. Fab hybrids containing a specific Fd fragment and a nonspecific L chain similarly reacted with antigen and remained in the circulation complexed to antigen. In contrast, L chains and Fab hybrids containing a specific L chain and a nonspecific Fd fragment did not react with antigen in vivo and were rapidly eliminated in both presence and absence of antigen. H chains remained in the circulation of rabbits in the absence of antigen, however, in the presence of antigen, more H chains which formed complexes with antigen remained in the intravascular space and were rapidly eliminated when the immune elimination of the antigen by the host occurred. Nonspecific H chains were rapidly eliminated from the circulaion of guinea pigs, whereas specific H chains remained in the circulation with the antigen. F (ab')2 fragments formed complexes with antigen near antibody equivalence and in antibody excess which were rapidly eliminated, however, less effectively than complexes formed near antibody equivalence with intact γG. Complexes formed in antibody excess between Fab fragments and H chains remained in the circulation at all concentrations studied and were eliminated at the rate of antigen. The role of the Fc fragment in the immune elimination of antigen-antibody complexes is discussed.

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