Summary
The secretory proteins of the larval salivary gland of some Chironomus species were analysed according to a method developed by Grossbach (1969). After reduction of the disulphide bonds and alkylation the secretion of Chironomus thummi was separated by disc electrophoresis at acrylamide concentrations of 4.8 to 9.5% into seven main and some minor fractions. By increasing the acrylamide concentration up to 20% nine main fractions could be resolved. In addition to these high molecular weight structural proteins a number of proteins soluble in simple buffer solutions and separable at pH 8.8 in a 15% acrylamide gel are present in the secretion but only to a very small amount.
The electrophoretic pattern of the secretory proteins of Chironomus strenzkei, Ch. luridus and Ch. obtusidens are qualitatively the same as the Ch. thummi pattern. Some quantitative differences may exist. In the secretion of Chironomus plumosus at least eleven main fractions were detected in 20% acrylamide gels. A comparison between the number of Balbiani rings of the salivary gland chromosomes and the number of main protein fractions in the salivary gland secretion yielded no direct correlation.
The results are discussed in respect to the question wether the major puffs of the gland, the Balbiani rings, encode the major products of the gland, the secretory proteins.
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Abbreviations
- BR:
-
Balbiani ring
- bis:
-
N,N′-Methylenebisacrylamide
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Communicated by C. Auerbach
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Wobus, U., Panitz, R. & Serfling, E. Tissue specific gene activities and proteins in the Chironomus salivary gland. Molec. Gen. Genet. 107, 215–223 (1970). https://doi.org/10.1007/BF00268696
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DOI: https://doi.org/10.1007/BF00268696