Abstract
Acid-soluble ribosomal proteins from cysts of Artemia salina were separated by high-resolution polyacrylamide gel electrophoresis at pH 4.3. Three distinct protein bands, occurring in different parts of the electrophoretic pattern, were used for immunization in rabbits, and the γ-globulin fractions of the antisera were prepared. These preparations produced precipitation lines in agarose gel with protein extracted from whole 80S ribosomes and from 60S and 40S ribosomal subunits. With γ-globulin preparations from non-immune or anti-ovalbumin sera no reactions were obtained. In gel diffusion experiments the three γ-globulin preparations were reacted with the corresponding antigens in homologous and heterologous combinations, as well as with other disc-electrophoretic fractions of Artemia ribosomal proteins. Precipitation lines were formed in all combinations. Immunological precipitates were also obtained with rat ribosomal protein. 125I-labelled γ-globulins against the ribosomal proteins reacted to a very limited extent with intact 80S ribosomes, and only slightly more with EDTA-treated ribosomes. The amino acid incorporating activity of the ribosomes was not impaired by preincubation with the γ-globulins.
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