| Literature DB >> 2381871 |
G Gäde1, G Rosiński.
Abstract
A hypertrehalosemic neuropeptide from the corpora cardiac of the two tenebrionid beetle species, Tenebrio molitor and Zophobas rugipes, was purified by high performance liquid chromatography, and its sequence determined by pulsed-liquid phase sequencing employing Edman degradation after deblocking enzymatically the N-terminal pyroglutamate residue. Additionally, the C-terminus of the peptide was blocked as shown by the lack of breakdown using carboxypeptidase. In both species an identical octapeptide, designated Tem-HrTH, with the following amino acid sequence, was found: pGlu-Leu-Asn-Phe-Ser-Pro-Asn-Trp-NH2. This primary sequence has an 88% homology with the hypertrehalosemic hormone I (Pea-CAH-I) from the American cockroach as well as with the red pigment-concentrating hormone (RPCH) of prawns. Injection of the synthetic peptide into larvae or young adults of T. molitor or adult Z. rugipes increases the hemolymph carbohydrate levels in a dose-dependent manner. Thin layer chromatography identified the elevated sugar component of the hemolymph as the disaccharide trehalose. Carbohydrate release from larval fat body in vitro was also shown upon administration of a low concentration of synthetic Tem-HrTH.Entities:
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Year: 1990 PMID: 2381871 DOI: 10.1016/0196-9781(90)90042-4
Source DB: PubMed Journal: Peptides ISSN: 0196-9781 Impact factor: 3.750