The solution structure of molt-inhibiting hormone from the Kuruma prawn Marsupenaeus 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 WJ, Aida K, Terauchi A, Sonobe H, Nagasawa H.
Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma
prawn Penaeus japonicus.
Peptides. 1996;17(2):197-202.

Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus.

Molt-inhibiting hormone precursor (MIH) (PeJ-SGP-IV)

The Solution Structure Of Molt-Inhibiting Hormone From The Kuruma Prawn