Biochemical characterization of a vasopressin-like neuropeptide in Locusta migratoria. Evidence of high molecular weight protein encoding vasopressin sequence.

The biochemical characterization of a diuretic neurohormone, immunologically related to the mammalian vasopressin (AVP) and present in Locusta migratoria has been performed. The results have been obtained using an AVP radioimmunoassay as method of detection and quantification. The "AVP like" molecule exhibits the same C terminal moiety: the tetrapeptide 1/2 Cys-PrO-Arg-Gly NH2. 125I-radiolabelling allows us to demonstrate the presence of a tyrosyl residue. The molecular weight of this molecule is estimated by gel filtration to 2500 +/- 400 Daltons. The isoelectric point is 7.5 and the electrophoretic migration lead to conclude to the presence of amino acid residues lacking in the vasopressin hormone. We have demonstrated the presence of a vasopressin sequence included in high molecular weight protein which have been quantified in suboesophageal ganglion (biosynthetic site) and in the nervous ventral cord (release site).