title: Complete primary structure of the molt-inhibiting hormone (MIH) of the Mexican crayfish Procambarus bouvieri (Ortmann).
abstract: The amino acid sequence of MIH was elucidated by means of digestions with specific proteases, manual Edman degradation, and mass spectrometry. MIH consists of a 72-residue peptide chain (molecular mass 8322 Da) with six cysteines forming three disulfide bridges that connect residues 7-43, 23-39, and 26-52. It has blocked N- and C-termini and lacks tryptophan, histidine, and methionine. MIH shows striking similarity to the crustacean hyperglycemic hormone (CHH) isomorphs of Procambarus bouvieri (90% identity) and to the MIH from Homarus americanus (79% identity) and Penaeus vannamei (46% identity). It is also related to the MIH from Carcinus maenas (28% identity) and Callinectes sapidus (28% identity).
authors: Department of Biochemistry, Instituto Nacional de la Nutrición Salvador Zubirán, Tlalpan, Mexico City, Mexico.
authors: M B
authors: MB
authors: Aguilar
authors: R
authors: R
authors: Falchetto
authors: J
authors: J
authors: Shabanowitz
authors: D F
authors: DF
authors: Hunt
authors: A
authors: A
authors: Huberman
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003400:Astacoidea / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry* / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin / Q000378:metabolism
chemical_list: D000596:Amino Acids; D009479:Neuropeptides; D010446:Peptide Fragments; C101529:molt-inhibiting hormone, crayfish; D002918:Chymotrypsin; D014357:Trypsin