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Abstract
A previous paper described the purification of a lectin induced in the hemolymph of larvae of Sarcophaga peregrina (flesh-fly) on injury of their body wall (Komano, H., Mizuno, D., and Natori, S. (1980) J. Biol. Chem. 255, 2919-2924). This paper describes cDNA cloning and the complete nucleotide sequence of the gene for Sarcophaga lectin. Although active lectin consists of alpha and beta subunits in a molar ratio of 2:1, the fat body of injured larvae was found to contain only mRNA for the alpha subunit, suggesting that these two subunits are derived from a common gene and that the alpha subunit is converted to the beta subunit post-translationally. The alpha subunit was found to consist of 260 amino acid residues with an additional signal sequence of 19 or 23 amino acid residues.
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