Abstract
Past research on diapause-inducing substances of the silkworm has isolated an extremely lipophilic peptide and demonstrated its unique characteristics. In the present work, similar lipophilic proteins were searched for in the shell of the shrimp, Pandalus borealis, and one novel protein, Pb CP-12.7, was isolated. Its structure comprising 126 amino acids was revealed by a combination of a sequence analysis and the enzymic fragmentation technique. Pb CP-12.7 is unique in that it was insoluble in neutral-slightly basic water, but highly soluble in some organic solvents. It contained an abundance of hydrophobic amino acids and repeating sequences. In addition, it was adsorbed to chitin, a major component of the shell of the shrimp.
