Premium
Preliminary characterization of glycogen phosphorylase activating hormone and adipokinetic hormone from Manduca sexta corpora cardiaca
Author(s) -
ZIEGLER ROLF,
GÄDE GERD
Publication year - 1984
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1111/j.1365-3032.1984.tb00702.x
Subject(s) - manduca sexta , adipokinetic hormone , sphingidae , biology , locust , glycogen phosphorylase , sephadex , biochemistry , acrididae , glycogen , endocrinology , medicine , insect , botany , orthoptera , enzyme , fat body , zoology , gene
. An attempt was made to separate glycogen phosphorylase activating hormone (GPAH) and adipokinetic hormone (AKH) from the corpora cardiaca (CC) of the moth Manduca sexta (Lepidoptera: Sphingidae) by separating extracts of CC on various chromotographic media, but it was not possible to conclude whether GPAH and AKH are activities of one or of two different peptides. Both activities elute together from glass beads, from Sephadex G‐25 and from Sephadex LH‐20 columns. In the separation experiments with glass beads and G‐25 the activities eluted as a single peak, but using LH‐20 we found two peaks exhibiting both activities. The major peak eluted at 1.25 × V t , which is very similar to locust AKH, while the smaller second peak eluted at O.74 × V t . Cross injections of CC extracts from M. sexta into Locusta migratoria and CC extracts from L. migratoria into M. sexta suggest that GPAH and the AKH from M. sexta are not identical with the decapeptide AKH from locusts.