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J. Biol. Chem., Vol. 261, Issue 4, 1616-1623, 02, 1986
BS Rothman, DH Hawke, RO Brown, TD Lee, AA Dehghan, JE Shively and E Mayeri
The atrial gland of the marine mollusk Aplysia californica contains several
biologically active peptides that are thought to be important in
reproductive function. In the present study, three novel peptides, which we
named califin A, B, and C, were purified from extracts of atrial glands by
high performance liquid chromatography, and their primary structures were
determined. Each consists of a 36-residue subunit bound by a single
disulfide bond to an 18-residue subunit. The large subunits differ from
each other by one or two residues, whereas the small subunits are
identical. The large subunits are 78-83% homologous to egg-laying hormone
(ELH), a 36-residue peptide synthesized by the neuroendocrine bag cells of
Aplysia. Like ELH, the califins excite LB and LC cells of the abdominal
ganglion and cause egg laying when injected into sexually mature animals.
Based on previously described DNA sequence data, each califin is likely to
be derived from one of several precursor proteins that are encoded by
members of the ELH gene family. Califin A is encoded on the peptide A
precursor, and califin B may be encoded on the peptide B precursor. No gene
encoding califin C has been sequenced. Because peptides A and B are also
biologically active, the precursors encoding them and califins A and B are
polyproteins. The possible role of atrial gland peptides as pheromones is
discussed.
Isolation and primary structure of the califins, three biologically active egg-laying hormone-like peptides from the atrial gland of Aplysia californica
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