Abstract
The salivary proteins of Chironomus thummi larvae were separated by SDS gel electrophoresis and characterized by immunological techniques. As a result, five protein fractions (sp-220, sp-180, sp-35, sp-18, and sp-16) with molecular weights Mr=220000, 180000, 35000, 18000 and 16000 were identified in 6%–20% polyacrylamide gradient gels. In addition, three giant proteins fractions (molecular weights exceeding Mr=800000) were detected in composite polyacrylamide-agarose gels. Crossed immunoelectrophoresis allowed us to identify five immunochemically dissimilar organ-specific antigen fractions in the salivary gland secretion. Data were obtained indicating that the protein fractions, sp-220, sp-180, sp-35, sp-18, and sp-16, are immunochemically and structurally similar. The giant secretory proteins and the secretory fractions with low molecular weights were found to be immunochemically unrelated.
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Kopantzev, E.P., Karakin, E.I. & Kiknadze, I.I. Tissue-specific secretory proteins of the salivary glands of Chironomus thummi An electrophoretic and immunochemical analysis. Chromosoma 92, 283–289 (1985). https://doi.org/10.1007/BF00329811
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DOI: https://doi.org/10.1007/BF00329811