Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractInduced responses to grazing by an insect herbivore (Acentria ephemerella) in an immature macrophyte (Myriophyllum spicatum): an isotopic study    Next AbstractDoes a pheromone-like factor from the nestling rabbit stimulate impregnation and maturation in the rabbit flea? »

J Biol Chem


Title:"Isolation and primary structure of the califins, three biologically active egg-laying hormone-like peptides from the atrial gland of Aplysia californica"
Author(s):Rothman BS; Hawke DH; Brown RO; Lee TD; Dehghan AA; Shively JE; Mayeri E;
Address:
Journal Title:J Biol Chem
Year:1986
Volume:261
Issue:4
Page Number:1616 - 1623
DOI:
ISSN/ISBN:0021-9258 (Print) 0021-9258 (Linking)
Abstract:"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"
Keywords:"Amino Acid Sequence Animals Aplysia/*analysis/physiology Binding Sites Chromatography, High Pressure Liquid Female Invertebrate Hormones/pharmacology Oviposition/drug effects Peptides/analysis/*isolation & purification/pharmacology Protein Precursors/meta;"
Notes:"MedlineRothman, B S Hawke, D H Brown, R O Lee, T D Dehghan, A A Shively, J E Mayeri, E eng Comparative Study 1986/02/05 J Biol Chem. 1986 Feb 5; 261(4):1616-23"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024