Preparation of tritiated oostatic peptides for study of radioactivity incorporation in flesh fly Neobellieria bullata

A series of insect oostatic peptides containing 3,4-dehydroproline in the C-terminal part or inside of the peptide chain was synthesized and tritiated by addition of ³H₂ to double bond of 3,4-dehydroproline residue. ³H-label was introduced also into tyrosine residue of oostatic tetra- and pentapeptides by isotopic exchange of benzyl β-hydrogens. In this way, three types of tritiated peptides were prepared, different in the radiolabeled amino acid position: [³H] Tyr-Asp-Pro-Ala-OH, H-Tyr-Asp-[³H] Pro-Ala-OH, [³H] Tyr-Asp-Pro-Ala-Pro-OH, H-Tyr-Asp-[³H] Pro-Ala-Pro-OH, H-Tyr-Asp-Pro-Ala-[³H] Pro-OH, H-Tyr-Asp-Pro-Ala-Pro₅-[³H] Pro-OH and H-Asp-[³H] Pro-OH. These peptides made possible a highly sensitive comparative study on radioactivity incorporation into head and ovaries of the flesh fly Neobellieria bullata, which revealed this process to proceed differently. The reasons of the found differences are discussed.