Abstract
The eclosion hormone (EH) of Manduca sexta is a 62 amino acid peptide which causes the behavioral and physiological changes that occur at ecdysis. EH was purified from the corpora cardiaca-corpora allata (CC-CA) complexes from pharate adult moths using acidic methanol extraction followed by two high performance liquid chromatography separation steps. One CC-CA complex was found to store about 3.5 ng of EH. Different techniques for estimating the molecular weight of the peptide, gel filtration chromatography and SDS-urea polyacrylamide electrophoresis, gave values of about 10 and 4 kD, respectively. Both were significantly different from the calculated molecular weight of 6813 dalton. The experimentally determined pI of the peptide was 4.8. Treatment of EH with various reagents showed that intact disulfide bridges are required for biological activity.
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