Synthesis of Lens Protein in vitro.

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Abstract
RNA was isolated from calf lens polysomes and crude nuclear preparations. Template activity, base composition, sedimentation behaviour, and electrophoretic properties were compared with corresponding RNA fractions from rat liver. 8–9‐fold stimulation of amino acid incorporation was obtained in the cell‐free test system derived from Escherichia coli. Template activity was widely distributed throughout sucrose density gradients. However, the major activity consistently was found at the bottom of the tubes. All fractions from the gradient revealed a heterogeneous pattern when subjected to polyacrylamide gel electrophoresis. The bottom fraction constistently showed a diffuse pattern instead of discrete bands. Only RNA fractions extracted at 65° and at pH 8.3 showed a G‐C content which was significantly different from ribosomal RNA.

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