The neuropeptidergic bag cells of the marine mollusc Aplysia californica ar
e involved in the egg-laying behavior of the animal, These neurosecretory c
ells synthesize an egg-laying hormone (ELH) precursor protein, yielding mul
tiple bioactive peptides, including ELH, several bag cell peptides (BCP) an
d acidic peptide (AP), While immunohistochemical studies have involved a nu
mber of species, homologous peptides have been biochemically characterized
in relatively few Aplysiidae species. In this study, a combination of matri
x-assisted laser desorption/ionization time-of-flight mass spectrometry (MS
) and electrospray ionization Fourier transform ion cyclotron resonance MS
is used to characterize and compare the ELH peptides from related opisthobr
anch molluscs including Aplysia vaccaria and Phyllaplysia taylori, The pept
ide profiles of bag cells from these two Aplysiidae species are similar to
that of A, californica bag cells. In an effort to characterize further seve
ral of these peptides, peptides from multiple groups of cells of each speci
es were extracted, and microbore liquid chromatography was used to separate
and isolate them. Several MS-based sequencing approaches are applied to ob
tain the primary structures of bag cell peptides and ELH, Our studies revea
l that alpha-BCPs are :100 % conserved across all species studied. In addit
ion, the complete sequences of epsilon-BCP and ELH of A. vaccaria were dete
rmined. They show a high degree of homology to their counterparts in A, cal
ifornica, with only a few amino acid residue substitutions.