| Abstract: | Protein synthesis (in particular, thyroglobulin) is studied in a cell-free system containing polyribosomes of thyroid gland. After the incubation with radioactive label, ribosomes were centrifugated, supernatant was dialyzed against 0.05 M Tris-HCl buffer, pH 7.2 for a night, concentrated by ficol and centrifugated in 5-20% linear sucrose gradient. 14C-radioactivity of 19S fraction (thyroglobulin) was shown to comprise about 25% of total radioactivity. The rest radioactivity was found in 3--8S fractions. The distribution of the radioactivity as it was shown by polyacrylamide gel electrophoresis is as follows: 27S--11.0%; 19S--14.2%; 12S--5.8% and 4S--7.6% of total radioactivity in polyacrylamide gel. It is supposed that two successive processes take place in thyroid gland: a synthesis of thyroglobulin subunits and an exchange of new synthesized subunits with presynthesized ones. |
