PURIFICATION AND PRIMARY STRUCTURE OF CERATOTOXIN-A AND CERATOTOXIN-B, 2 ANTIBACTERIAL PEPTIDES FROM THE FEMALE REPRODUCTIVE ACCESSORY-GLANDS OF THE MEDFLY CERATITIS-CAPITATA (INSECTA, DIPTERA)
D. Marchini et al., PURIFICATION AND PRIMARY STRUCTURE OF CERATOTOXIN-A AND CERATOTOXIN-B, 2 ANTIBACTERIAL PEPTIDES FROM THE FEMALE REPRODUCTIVE ACCESSORY-GLANDS OF THE MEDFLY CERATITIS-CAPITATA (INSECTA, DIPTERA), Insect biochemistry and molecular biology, 23(5), 1993, pp. 591-598
In the present article we report the purification and the amino acid s
equence of two antibacterial peptides present in the secretion of the
female reproductive accessory glands of the dipteran insect Ceratitis
capitata. Both peptides consist of 29 amino acid residues, are heat st
able, strongly basic and differ from each other for the substitution o
f two amino acids. Their primary sequence and predicted secondary stru
cture are related to other families of peptides known to have lytic an
d/or antibacterial activity. We propose the name ceratotoxins (from Ce
ratitis) for these antibacterial peptides.