title: Insect immunity. The primary structure of the antibacterial protein attacin F and its relation to two native attacins from Hyalophora cecropia.
abstract: The attacins are antibacterial proteins present in the hemolymph of the pupae of the silk moth Hyalophora cecropia after bacterial infection. We present the primary structure of one attacin, the F form. We show that this protein is derived by proteolysis from the native protein, attacin E. Using a method for rapid purification from the hemolymph of immunized pupae of the neutral attacin E and a basic attacin, both proteins were found in freshly collected immune hemolymph. We conclude that they are the native products of two attacin genes, the existence of which was inferred from the isolation of two cDNA clones as described in the accompanying paper. The two proteins, which differed in their pIs (7 and 9), were found to have similar mol. wts. (20 000) and closely related primary structures, displaying a total of 40 amino acid substitutions, 12 of which were of a non-conservative nature.
authors.affiliation: The Biomedical Center, Uppsala University, Box 575, S-751 23 Uppsala, Sweden.
authors.forename: A
authors.initials: A
authors.lastname: Engström
authors.forename: P
authors.initials: P
authors.lastname: Engström
authors.forename: Z J
authors.initials: ZJ
authors.lastname: Tao
authors.forename: A
authors.initials: A
authors.lastname: Carlsson
authors.forename: H
authors.initials: H
authors.lastname: Bennich