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Identification of tissue-specific antigens and concanavalin A receptors on rat epidermal cells using a radio-immunoprecipitation method.

Iodination with lactoperoxidase - 125I- - H2O2 was used to label surface components of rat epidermal cells. Lysis of the cells in non-idet P40 resulted in the solubilization of tissue-specific antigens and of concanavalin A receptors. These specificities were demonstrated using a radio-immunoprecipitation method. The tissue-specific antigens were recognized using absorbed rabbit anti-rat epidermal cell sera (Lloyd & Darnule 1974); they reacted with two low molecular weight components in the lysate (9,000 and 12,000 daltons). Concanavalin A reacted with three major components. Two had high molecular weights (75,000 and 95,000 daltons). The possibility that one of these components was radioiodinated lactooperoxidase, which would have reacted with concanavalin A, was disproved. Another component (which occasionally appeared as two peaks) was similar in size to the species detected by the tissue-specific antisera. Their non-identity was, however, demonstrated by the finding that the two specificities could be precipitated independently of each other.