Abstract
In order to study the character and properties of antigen-specific receptors on lymphocyte surfaces, an immunoadsorption method based on the principle described by Kiefer (1973, 1975) has been developed. This method permits isolation of receptors from rabbit and pig spleen and lymph node cells in quantities sufficient for basic analyses. Isolated receptors represent a mixture of two groups of antigen binding molecules. Both groups react with corresponding anti-idiotypic antisera but only one of them reacts with antisera to serum immunoglobulins. These two fractions can be separated using an immunoadsorbent with bound antibodies to serum immunoglobulins. In the fraction bearing immunoglobulin determinants, the presence of IgM and IgG but not IgA has been detected. The IgG receptors and IgG antibodies in the serum of the same animal had different isoelectrofocusing spectra. The origin of the other antigen-binding fraction remains to be established. The results obtained with antisera to the ‘constant part’ of this molecule confirmed that it does not carry conventional immunoglobulin determinants.
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