Cell-free synthesis and immunological characterization of salivary proteins from Chironomus tentans.
We have isolated the salivary proteins of the larva of the harlequin fly Chironomus tentans, and characterized its constituents by gel electrophoresis and immunological techniques. The detailed composition of saliva from individual animals is shown to be very variable, but four main protein groups can be defined. The largest, Fraction A, comprises up to five species, with molecular weights of between 820,000 and 700,000 Daltons. It includes at least two distinct antigenic species. This finding is discussed in the context of the known heterogeneity of the 75S RNA fraction which is transcribed in the Balbiani rings 1 and 2. -- The other prominent protein classes in isolated saliva range in size from 230,000 down to less than 20,000 Daltons. -- We have also employed antiserum against salivary proteins to investigate the products of in vitro translation of salivary gland RNA in the rabbit reticulocyte lysate system. A broad spectrum of polypeptide species is obtained which are immunologically related to salivary components, including species of over 300,000 Daltons. These latter are interpreted as unfinished Fraction A polypeptides resulting from incomplete translation of 75S RNA from BR1 and BR2. Evidence is presented to demonstrate that other salivary proteins, apart from Fraction A, are faithfully translated in the reticulocyte lysate.
D000818:Animals; D002474:Cell-Free System; D002683:Chironomidae / Q000235:genetics*; D004175:Diptera / Q000235:genetics*; D000939:Epitopes; D066298:In Vitro Techniques; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012469:Salivary Glands / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000032:analysis / Q000235:genetics* / Q000276:immunology
D000939:Epitopes; D012471:Salivary Proteins and Peptides