Abstract
Injection of rabbit spleen ribonuclease, which had been isolated in a pure state by physicochemical procedures developed in this laboratory, into a sheep elicited the production of ‘monospecific’ antibodies, as judged by the formation of a single precipitin band on immunodiffusion and on immunoelectrophorersis. Reverse immunosorbents were readily prepared by insolubilizing the antibodies with ethyl chloroformate or ethylene maleic ahydride. These immunosorbents combined specifially with the ribonuclease present in a crude extract of rabbit spleen. The ribonuclease was eluted in a pure state and with a yield of 86 per cent with 0·4 M glycine-HCl buffer at pH 2.
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