Current Microbiology, Vol.51, No.6, 367-371, 2005
Purification and characterization of Cry1Ac toxin binding proteins from the brush border membrane of Helicoverpa armigera midgut
Several Cry1Ac binding proteins from midgut of Helicoverpa armigera were purified using toxin-affinity chromatography. Enzyme assays showed that the purified proteins had strong aminopeptidase activity. The N-terminal sequences confidently identified a 124-kDa binding protein as an aminopeptidase N (APN), and some similarity suggests that a 162-kDa binding protein may also be an APN. Two minor binding proteins were not characterized.