Summary
Secretory proteins isolated from the lumen of the Chironomus thummi salivary gland were labelled with radioactive amino acids in vivo and in vitro. Under both conditions all but one of the electrophoretically separated fractions became labelled, the 6 prominent polypeptides already after 10–15 min of incubation. Differences in the labelling pattern during development from early 4th instar larvae to late prepupae were not detected.
After synthesis the secretory proteins are stored in the cytoplasm for different times until they are exported into the gland lumen.
None of the prominent protein fractions extracted only from the cells of the gland were found to be labelled even after labelling times up to 10 hrs. Therefore, it may be concluded that the Chironomus salivary gland synthesizes predominatly secretory proteins at least after the last larval moult.
Long-time treatment of whole larvae with actinomycin D has no striking effect on the protein synthesis of the gland.
Some of the results together with data from the literature led us to the speculation that changes of puff patterns (Balbiani rings excluded) do not reflect subsequent changes at the translational level.
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Wobus, U., Popp, S., Serfling, E. et al. Protein synthesis in the Chironomus thummi salivary gland. Molec. Gen. Genet. 116, 309–321 (1972). https://doi.org/10.1007/BF00270088
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DOI: https://doi.org/10.1007/BF00270088