Amino acid sequence of putative moult-inhibiting hormone from the crab Carcinus maenas.
Putative moult-inhibiting hormone (MIH) was isolated from sinus glands of the shore crab Carcinus maenas, and its primary structure determined by automated Edman degradation of endoproteinase derived peptide fragments. MIH is a 78 residue neuropeptide (deduced molecular mass 9181 Da) with three disulphide bridges and unblocked N- and C-termini. MIH shows some homology to the crustacean hyperglycemic hormone (CHH) neuropeptide family. However, consideration of the roles of various members of this group, together with sequence information recently reported, strongly suggests that these neuropeptides may be multifunctional.
Webster
S G
SG
School of Biological Sciences, University of Wales, Bangor, Gwynedd, U.K.
D000595:Amino Acid Sequence; D000818:Animals; D003386:Brachyura; D002849:Chromatography, Gas; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis; D004441:Ecdysterone / Q000037:antagonists & inhibitors; D010450:Endopeptidases; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008121:Nephropidae; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D016339:Spectrometry, Mass, Fast Atom Bombardment
D004220:Disulfides; D007447:Invertebrate Hormones; D010446:Peptide Fragments; C012445:molt-inhibiting hormone; D004441:Ecdysterone; D010450:Endopeptidases