Isolation and molecular characterization of a hyperglycemic neuropeptide from the sinus gland of the terrestrial isopod Armadillidium vulgare (Crustacea).

Important note: Information in this article was accurate in 1993. The state of the art may have changed since the publication date.

Isolation and molecular characterization of a hyperglycemic neuropeptide from the sinus gland of the terrestrial isopod Armadillidium vulgare (Crustacea).

Eur J Biochem. 1993 Feb 1;211(3):601-7. Unique Identifier : AIDSLINE MED/93170291
Martin G; Sorokine O; Van Dorsselaer A; Laboratoire de biologie animale URA 1452, Universite de; Poitiers, France.

Abstract: The major peptide from the sinus gland of the terrestrial isopod Armadillidium vulgare (Crustacea) has been extracted and purified by reverse-phase HPLC. This neuropeptide exhibited a high hyperglycemic activity and was therefore named A. vulgare crustacean hyperglycemic hormone (Arv-CHH). Its average molecular mass measured by mass spectrometry was 8729.3 Da. Its complete amino acid sequence was determined by a combination of Edman degradation and mass spectrometry. The N-terminal amino acid was found to be unblocked, the C-terminal residue was found amidated and none of the other 72 residues was affected by any post-translational modification. Disulfide bond assignment was made unambiguously by mass spectrometry and Edman degradation was performed on peptides produced by enzymatic cleavage. Relationships with other, similar neuropeptides from decapod sinus glands are discussed.

Keywords: Amino Acid Sequence Animal Chromatography, High Pressure Liquid *Crustacea Disulfides/CHEMISTRY/METABOLISM Invertebrate Hormones/CHEMISTRY/*ISOLATION & PURIF/PHARMACOLOGY Molecular Sequence Data Molecular Weight Nerve Tissue Proteins/CHEMISTRY/*ISOLATION & PURIF/PHARMACOLOGY Peptide Fragments/CHEMISTRY/METABOLISM Peptide Peptidohydrolases/METABOLISM Serine Proteinases/METABOLISM Spectrum Analysis, Mass Trypsin/METABOLISM JOURNAL ARTICLE
930530
M9350261

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