Abstract
The polypeptide composition of egg yolk proteins was analysed in 23 species of grasshoppers by means of SDS-PAGE. Each species has a distinguishable set of polypeptides, varying from three to seven (although most show five or six), which can be classified into two groups of high (H) and low molecular weight (L). The patterns can be interpreted following a two-gene model, each with three domains that codify two H and one L polypeptides. The results suggest strong rearrangements in vitellin during speciation and a later slowing in divergence due to functional constraints. Consequently, the vitellin polypeptide composition may be used for species identification but does not provide phylogenetic information above the genus level. Intraspecific variability was found only in Eyprepocnemis plorans, which appears to be quite recent from an evolutionary point of view, and in Chorthippus parallelus where the subspecies differentiation may be older. © 2002 The Linnean Society of London, Biological Journal of the Linnean Society, 2002, 75, 281–290.
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