Antibodies were raised in rabbits against 70S ribosomes, 50S and 30S ribosomal subunits individually. Purified immunoglobulins from the antiserum against each of the above ribosomal entities were tested for their capabilities of precipitating 70S, 50S and 30S ribosomes. The observations revealed the following: (i) The antiserum (IgG) raised against 70S ribosomes precipitates 70S ribosomes completely, while partial precipitation is seen with the subunits, the extent of precipitation being more with the 50S subunits than with 30S subunits; addition of 50S subunits to the 30S subunits facilitates the precipitation of 30S subunits by the antibody against 70S ribosomes. (ii) Antiserum against 50S subunits has the ability to immunoprecipitate both 50S and 70S ribosomes to an equal extent. (iii) Antiserum against 30S subunits also has the property of precipitating both 30S and 70S ribosomes. The differences in the structural organisation of the two subunits may account for the differences in their immunoprecipitability.

On sucrose gradient centrifugation, the ribosomal preparation from chloramphenicol-treated³²P labelledEscherichia coli AB301/105 (RNase III^-) showed the presence of a radioactive peak moving slower than the 70S ribosome; this peak disappeared on treatment with RNase III. The presence of precursor 30S RNA was shown in such preparations by affinity chromatography on a lysine-sepharose 4B column as well as polyacrylamide gel electrophoresis. Dialysis against low Mg^2± concentration followed by sucrose density gradient electrophoresis. Dialysis against dissociation of 70S ribosome into its subunits, did not lead to the dissociation of the precursor ribosome. However, the dissociation took place upon treatment with RNase III. A tentative model of coupled rRNA transcription and ribosome assembly has been presented.