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Biochem Mol Biol Int. 1994 Jul;33(4):751-8.

Inhibition of prophenoloxidase-activating enzyme from Bombyx mori by endogenous chymotrypsin inhibitors.

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  • 1Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.


Inhibitory activities for the activation of prophenoloxidase with its activating enzyme were detected in the gel-filtration fractions of hemolymph from Bombyx mori. The fractions with the highest activity contained chymotrypsin inhibitors; CI-13a, 13b, and 13c. They inhibited the activation of prophenoloxidase. The activating enzyme affected a synthetic substrate for trypsin, Boc-Gln-Ala-Arg-MCA: Km = 0.62 mM. CI-13c partially suppressed the peptidase activity.

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