Soyez D, Noel P Y, Van Deijnen J E, Martin M, Morel A, Payen G G
Laboratoire de Neuroendocrinologie des Crustacés, URA 555 CNRS, Université Pierre et Marie Curie, Paris, France.
Gen Comp Endocrinol. 1990 Aug;79(2):261-74. doi: 10.1016/0016-6480(90)90112-y.
In order to characterize hyperglycemic peptides from the sinus gland of the lobster, Homarus americanus, a bioassay was developed with juvenile H. gammarus. This assay was used for determining the hyperglycemic activity of peptides perified by reversed-phase high-performance liquid-chromatography, from acidic extracts of sinus gland. The major peptides are eluted in three sets of two peptides. Among them, two pairs show hyperglycemic activity when assayed on lobster; when assayed on crayfish, three peptides are active. The less hydrophobic pair consists of basic peptides (pI: 8.7), with a MW of 8633 Da., determined by fast-atom bombardment mass spectrometry. The most hydrophobic pair consists of acid peptides (pI: 5.0), with a MW of 8577 Da. Amino acid composition of the hyperglycemic peptides shows strong homologies within each pair.