scholarly journals Antigen-specific T lymphocyte clones. III. Papain splits purified T suppressor molecules into two functional domains.

1982 ◽  
Vol 155 (4) ◽  
pp. 981-993 ◽  
Author(s):  
M Fresno ◽  
L McVay-Boudreau ◽  
H Cantor
Keyword(s):  
Antibody Response ◽  
T Lymphocyte ◽  
Sheep Erythrocyte ◽  
Variable Region ◽  
Binding Activity ◽  
Functional Domains ◽  
Antigen Binding ◽  
Constant Region ◽  
Foreign Proteins

Purified molecules (70,000 mol wt) from a T-suppressor (Ts) clone bind to sheep erythrocyte glycophorin and specifically suppress the response to this antigen. Papain splits purified 70,000-mol wt Ts molecules into two peptides: mol wt 45,000 and 24,000. The 45,000-mol wt peptide nonspecifically suppresses antibody response to several antigens and lacks antigen-binding activity. The 24,000-mol wt peptide does not suppress but retains antigen-binding activity. The results indicate that papain splits the Ts molecule into a "constant" region responsible for function and a "variable" region responsible for antigen-binding. Since binding of the 70,000-mol wt molecule to antigen also results in release of the 45,000 mol wt subunit, this cleavage may allow Ts molecules specific for one determinant to suppress immunity to complex foreign proteins.

scholarly journals Human rheumatoid factor crossidiotypes. I. WA and BLA are heat-labile conformational antigens requiring both heavy and light chains.

1986 ◽  
Vol 164 (5) ◽  
pp. 1809-1814 ◽  
Author(s):  
V Agnello ◽  
J L Barnes
Keyword(s):  
Rheumatoid Factor ◽  
Primary Structure ◽  
Binding Activity ◽  
Light Chains ◽  
Heat Denaturation ◽  
Antigen Binding ◽  
Rheumatoid Factors ◽  
Simple Method ◽  
Heat Labile

Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.

scholarly journals Broadly Distributed Chemical Reactivity of Natural Antibodies Expressed in Coordination with Specific Antigen Binding Activity

2003 ◽  
Vol 278 (22) ◽  
pp. 20436-20443 ◽  
Author(s):  
Stephanie Planque ◽  
Hiroaki Taguchi ◽  
Gary Burr ◽  
Gita Bhatia ◽  
Sangeeta Karle ◽  
...  
Keyword(s):  
Chemical Reactivity ◽  
Specific Antigen ◽  
Binding Activity ◽  
Natural Antibodies ◽  
Antigen Binding

Antibodies to Rotaviruses in Chickens' Eggs: A Potential Source of Antiviral Immunoglobulins Suitable for Human Consumption

PEDIATRICS ◽  
1988 ◽  
Vol 81 (2) ◽  
pp. 291-295
Author(s):  
Robert H. Yolken ◽  
Flora Leister ◽  
Siok-Bi Wee ◽  
Robin Miskuff ◽  
Steven Vonderfecht
Keyword(s):  
Binding Activity ◽  
Human Consumption ◽  
Antigen Binding ◽  
Rotavirus Gastroenteritis ◽  
Potential Source ◽  
Egg Products ◽  
Egg Yolks ◽  
The Individual ◽  
Antibody Levels ◽  
Infants And Young Children

The prevalence of antibodies to human rotaviruses in commercially available eggs and egg products that are suitable for human consumption was investigated. The yolks of virtually all of the individual eggs and pasteurized pooled egg preparations contain antirotavirus antibodies detectable by means of enzyme immunoassay systems. Also, the eggs and egg preparations are capable of inhibiting the growth of two strains of rotaviruses in tissue culture. Chromatographic studies indicated that the antigen-binding activity is limited largely to the immunoglobulin fractions of the egg yolks. The antibody levels in eggs can be increased by the immunization of hens with purified rotavirus preparations, and the immunoglobulins isolated from the eggs of immunized hens can prevent the development of rotavirus gastroenteritis in experimentally infected animals. Egg preparations might serve as a practical source of antiviral antibodies suitable for consumption by infants and young children.

Immunosuppression by Murine Sarcoma Virus (Moloney)

1970 ◽  
Vol 1 (3) ◽  
pp. 288-292
Author(s):  
S. P. Chan ◽  
W. A. Hook ◽  
W. Turner ◽  
M. A. Chirigos
Keyword(s):  
Antibody Response ◽  
Survival Time ◽  
Primary Tumor ◽  
Sheep Erythrocyte ◽  
Humoral Antibody ◽  
Secondary Tumors ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Erythrocyte Antigen ◽  
Murine Sarcoma

Infection of mice with the murine sarcoma virus (Moloney) markedly suppressed the humoral antibody response to sheep erythrocyte antigen injected 10 days after infection, when tumor size was maximal, and on day 26, when primary tumors had partially regressed. Humoral antibody response was also inhibited when antigen was injected at the time secondary tumors and metastases were evident. No significant suppression of humoral antibody was seen when mice were injected with sheep erythrocyte antigen 5 days after virus infection. Inhibition of the cellular immune response of murine sarcoma virus (Moloney)-infected mice, as measured by the increased survival time of skin grafts, was also determined. Mice that were infected 5 days prior to grafting demonstrated prolonged survival of grafts, suggesting a suppression of cellular immunity. These mice had a graft survival time 14 days greater than noninfected controls. No significant prolongation of graft survival was seen in mice grafted at the times of maximum primary tumor growth, of primary tumor regression, or when secondary tumors had appeared.

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