Determination of the amino acid sequence of the moult-inhibiting hormone from the edible crab, Cancer pagurus.
Putative moult-inhibiting hormone (MIH) from sinus glands of the edible crab Cancer pagurus was characterized by high-performance liquid chromatography, followed by fractional bioassay (inhibition of ecdysteroid synthesis by Y-organs) and immunoassay (using antisera raised against Carcinus MIH). This peptide was fully sequenced by automated Edman degradation of endoproteinase-derived fragments. C. pagurus MIH is a 78 residue peptide (M(r) 9194), with free N- and C-termini and three intrachain disulphide bridges. Comparison with previously published MIH sequences confirms a high degree of sequence identity (c. 80%), supporting the view that brachyurans (crabs), possess distinct, structurally similar MIH neuropeptides.
Chung
J S
JS
School of Biological Sciences, University of Wales Bangor, Gwynedd, UK.
Wilkinson
M C
MC
Webster
S G
SG
D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D003386:Brachyura / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007124:Immunoenzyme Techniques; D007447:Invertebrate Hormones / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification; D013058:Mass Spectrometry; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011863:Radioimmunoassay; D017421:Sequence Analysis; D014357:Trypsin
D007447:Invertebrate Hormones; D010446:Peptide Fragments; C012445:molt-inhibiting hormone; D014357:Trypsin; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase; C058921:endoproteinase Asp-N