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Biomedical subjects

T Ternynck

Publications and source records attributed to T Ternynck.

At least 73 records · Page 4Linked to original sources
PubMed1975

Synthesis of antibody and immunoglobulins without detectable antibody function in cells responding to horseradish peroxidase.

The kinetics of immunoglobulin-synthesizing cells (IFC) and antibody-forming cells (AFC) are compared in the popliteal nodes of mice challenged, in the hind footpads, with horseradish peroxidase (PO) in Freund's complete adjuvant. A rise in the number of IFC without antibody function precedes the appearance of AFC. IFC reach peak numbers 7 days before AFC. Control experiments show that the majority of IFC without antibody function are responding to PO and not to adjuvant. Kinetic and radioautographic data suggest that IFC arise by division and differentiation; however, the doubling time of AFC is too rapid to be accounted for by cell division alone. Double staining techniques revealed the presence of immunoglobulin and antibody in different compartments of the same cell in 5 to 15% of the AFC. It is postulated that some AFC are recruited, possibly from cells already synthesizing immunoglobulin determinants.

Animals↗
PubMed1974

Similar idiotypes in antibody-forming cells and in cells synthesizing immunoglobulins without detectable antibody function.

The occurrence of immunoglobulins with and without antibody specificity and with and without idiotypic specificity was studied, by use of enzyme-labeled antigen and antibodies, in lymph node cells of rabbits immunized with horse-radish peroxidase and hen ovalbumin. Some cells, containing immunoglobulins without detectable antibody function, were shown to contain idiotypes similar to those found in antibody-producing cells.

Alkaline Phosphatase↗
PubMed1973

Intracellular distribution of antibody in immunocytes responding to primary challenge with horseradish peroxidase.

A new improved technic was used to follow the development of, and the intracellular antibody distribution in antiperoxidase antibody-forming cells (AFC) of the mouse popliteal lymph nodes responding to primary stimulation with horse-radish peroxidase (HRP). The first AFC were found 6 to 8 days after immunization and were all plasma cells. Antibody was concentrated in the Golgi complexes and in a few cisternae of rough endoplasmic reticulum. Subsequently, an increasing proportion of the AFC were filled with antibody, and with time the numbers of full cells and the intensity with which they stained increased. Kinetic studies of the cell changes in the lymph node medulla suggest that lymphoid cells proliferate, differentiate into plasma cells, and are then recruited as AFC. Furthermore, it was concluded that the changing intracellular distribution of antibody represents the gradual filling of the AFC with specific antibody.

Animals↗
PubMed1973

Intracellular distribution of antibody in immunocytes responding to secondary challenge with horseradish peroxidase.

A new improved immunoperoxidase method was used to study the antiperoxidase antibody-forming cells (AFC) in the medullae of mouse popliteal nodes after a second challenge with horseradish peroxidase (HRP). Two populations of AFC were found: a) A stable nondividing background population of mature plasma cells whose content of antibody increased 3 days after challenge and b) A new population of cells which increased in number exponentially between 18 hours and 5 days after challenge. In contrast with the first response, the new AFC included many stimulated lymphoid cells, significant numbers of small lymphocytes, and plasma cells. The results suggest that the morphology of the AFC found in the first and second responses reflects the stage in their developmental cycle at which the precursor cells are recruited into the AFC population. More than 90% of the AFC arising between 18 hours and 3 days after challenge had antibody in their perinuclear cisternae, and their cisternae of rough endoplasmic reticulum were rapidly filled with antibody. The striking differences between the intracellular localisation of antibody during the first and second responses are discussed.

Animals↗
PubMed1971

Effect of electrolytes and of distilled water on antigen-antibody complexes.

Specific immune precipitates dissolve in concentrated solutions of alkali-metal halides, and of alkaline-earth-metal halides and thiocyanates. The quantity of protein dissolved depends on the nature of the antigen-antibody system, on the proportion of the antigen in the precipitate, and on the avidity of the antibody. The extent of solubilization is a function of the temperature, of the volume of solution used and of the concentration of the ions in the solution, and also depends on the nature of these ions. The dissolving power of bivalent cations is greater than that of monovalent ones, and is as follows: Mg(2+)[unk]Ba(2+)[unk]Ca(2+)[unk]Sr(2+). Antigen-antibody complexes and free antibodies, but no free antigen, are detected in supernatants of specific precipitates dissolved in solutions of electrolytes of low ionic strength. Antigen-antibody complexes, free antibodies and also free antigen are detected in supernatants of specific precipitates dissolved in solutions of electrolytes of high ionic strength. Comparable results are obtained when the electrolyte solutions are studied for their effect on the bonds formed between an antibody and its corresponding immunosorbent. Moreover, in the latter case, 50% of the fixed antibodies could be recovered by elution with distilled water.

Animals↗