Storage proteins in the olive fruit fly, Dacus oleae: Characterization and immunological studies

Abstract

Dacin, a storage protein, has been isolated from the olive pest Dacus oleae. By native gel electrophoresis, two major bands of dacin could be observed. SDS gel electrophoresis has revealed, that two polypeptides α and β, are responsible for the formation of the two major bands found during native gel electrophoresis. The molecular weight of the α and β polypeptides was estimated to be 82,000 and 84,000 respectively. By immunological analysis, it was established that dacin is homologous to the other storage proteins, calliphorin and ceratitin. Dacin is first observed in small amounts in early third instar larvae and increases dramatically in white pupae and 4-day-old pupae. It decreases during the middle and late pupal stages and in 2-day-old adults only traces could be detected.