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)

Citation
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
Citations number
48
Categorie Soggetti
Entomology,Biology
ISSN journal
09651748
Volume
23
Issue
5
Year of publication
1993
Pages
591 - 598
Database
ISI
SICI code
0965-1748(1993)23:5<591:PAPSOC>2.0.ZU;2-3
Abstract
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.