Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera.

@article{Bania1999PrimarySA,
  title={Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera.},
  author={Jacek Bania and Damian Stachowiak and Antoni Polanowski},
  journal={European journal of biochemistry},
  year={1999},
  volume={262 3},
  pages={680-7}
}
A member of the Ascaris inhibitor family exhibiting anti-cathepsin G and anti-chymotrypsin activity was purified from the larval hemolymph of the honey bee (Apis mellifera). Three forms of the inhibitor, designated AMCI 1-3, were isolated using gel filtration and anion-exchange chromatographies followed by reverse-phase HPLC. The amino-acid analyses indicated that AMCI-1 and AMCI-2 have an identical composition whereas AMCI-3 is shorter by two residues (Thr, Arg). All three forms contain as… CONTINUE READING

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