Isolation and characterization of the novel lipophilic protein, Pb CP-12.7, from the shell of the pink shrimp, Pandalus borealis.
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.
Suzuki
K
K
Faculty of Bioresources, Mie University, Tsu, Japan.
Okamori
M
M
Katsuzaki
H
H
Komiya
T
T
Imai
K
K
D000327:Adsorption; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D002686:Chitin / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000737:chemistry; D008969:Molecular Sequence Data; D033542:Pandalidae / Q000737:chemistry*; D010449:Peptide Mapping; D011487:Protein Conformation
D002352:Carrier Proteins; C438908:Pb CP-12.7 protein, Pandalus borealis; D002686:Chitin; D002918:Chymotrypsin; C117608:alpha-chymotrypsin