Abstract

Various species of rapidly labelled, informational ribonucleoproteins can be isolated from homogenates of newt oocytes. Polyribosome-associated ribonucleoprotein can be separated from heterogeneous nuclear ribonucleoprotein and free cytoplasmic ribonucleoprotein by sucrose gradient centrifugation. The polyribosome-associated ribonucleoprotein can be released from the ribosome complex by treatment with low concentrations of EDTA and has the following properties: 1. 1. It is rapidly labelled with [ 3H]uridine under condition (incubation of oocytes for 4 h and less at 20°C) where there is no detectable labelling of ribosomal subunits. 2. 2. It is heterogeneous in size, consisting of particles most of which sediment between 40 S and 80 S. 3. 3. Its sedimentation coefficient is related directly to the size of the polyribosomal complex from which it is derived. 4. 4. Its density ranges from 1.35 g/cm 3 to 1.55 g/cm 3 irrespective of size. This indicates protein to RNA ratios of 4:1 to 2:1. 5. 5. It is active, when complexed with ribosomes, in cell-free protein synthesis. It is concluded that this polyribosome-associated ribonucleoprotein is functional messenger and its role in oocyte maturation is discussed.

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