Complete primary structure of the molt-inhibiting hormone (MIH) of the Mexican crayfish Procambarus bouvieri (Ortmann).
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).
Aguilar
M B
MB
Department of Biochemistry, Instituto Nacional de la Nutrición Salvador Zubirán, Tlalpan, Mexico City, Mexico.
Falchetto
R
R
Shabanowitz
J
J
Hunt
D F
DF
Huberman
A
A
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
D000596:Amino Acids; D009479:Neuropeptides; D010446:Peptide Fragments; C101529:molt-inhibiting hormone, crayfish; D002918:Chymotrypsin; D014357:Trypsin