Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus.
Six major peptides (Pej-SGP-I-VI) that belong to the CHH family have been isolated from the sinus gland extracts of the kuruma prawn Penaeus japonicus. By in vitro assay using the Y-organ of the crayfish Procambarus clarkii, Pej-SGP-IV was found to be active in inhibiting ecdysteroid synthesis. We determined the complete amino acid sequence. Pej-SGP-IV consists of 77 amino acid residues, with both free aimno- and carboxyl-termini. The sequence of Pej-SGP-IV shows considerable similarity to that of MIH of the shore crab Carcinus maenas and less similarity to Pej-SGP-III, whose sequence has been previously determined.
Yang
W J
WJ
Department of Fisheries, Faculty of Agriculture, University of Tokyo, Japan.
Aida
K
K
Terauchi
A
A
Sonobe
H
H
Nagasawa
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D018978:Molting / Q000187:drug effects*; D009479:Neuropeptides; D033561:Penaeidae / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D009479:Neuropeptides; C101066:Pej-SGP-IV protein, Penaeus japonicus; D011506:Proteins