On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia.
Diapausing pupae of Cecropia respond to a bacterial infection by the selective synthesis of RNA and 15-20 hemolymph proteins. Of these we have purified lysozyme and two classes of antibacterial proteins called cecropins and attacins. The primary structure has been determined for the lysozyme, one attacin and five cecropins. We have also prepared a cDNA bank, isolated and sequenced clones corresponding to the lysozyme, the two main attacins and one cecropin. The results of these structural studies are briefly summarized. Finally we review the solid phase synthesis of cecropin A and B and 9 analogs of cecropin A.
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D004247:DNA / Q000235:genetics; D007301:Insect Hormones / Q000235:genetics / Q000302:isolation & purification*; D019476:Insect Proteins; D007915:Lepidoptera / Q000032:analysis*; D009036:Moths / Q000032:analysis* / Q000235:genetics; D009113:Muramidase / Q000235:genetics / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid
D023181:Antimicrobial Cationic Peptides; D007301:Insect Hormones; D019476:Insect Proteins; C039711:attacin antibacterial protein, insect; C031161:cecropin A; C031162:cecropin B protein, Insecta; C036149:cecropin D protein, Hyalophora cecropia; D004247:DNA; D009113:Muramidase