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.
Liao
Chunyan
C
CSIRO Entomology, GPO Box 1700, ACT 2601, Australia.
Trowell
Stephen C
SC
Akhurst
Ray
R
D000626:Aminopeptidases / Q000032:analysis / Q000302:isolation & purification; D000818:Animals; D001426:Bacterial Proteins; D018826:CD13 Antigens / Q000235:genetics; D002846:Chromatography, Affinity; D004064:Digestive System / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D019476:Insect Proteins / Q000302:isolation & purification*; D008871:Microvilli / Q000737:chemistry*; D009036:Moths / Q000737:chemistry*; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; C095416:Cry toxin receptors; D019476:Insect Proteins; D011956:Receptors, Cell Surface; D000626:Aminopeptidases; D018826:CD13 Antigens