Protease inhibitor controls prophenoloxidase activation in Manduca sexta

FEBS Letters

Saul, Steven J.¹  Sugumaran, Manickam¹ 

[1] Department of Biology, University of Massachusetts, Harbor Campus, Boston, MA 02125, USA

关键词: Prophenoloxidase Enzyme activation Enzyme inhibitor Proteolysis Insect immunity (Manduca sexta);   

DOI  :  10.1016/0014-5793(86)81543-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prophenoloxidase from the hemolymph of tobacco hornworm Manduca sexta can be activated by a specific activating enzyme found in the cuticle. Inhibition studies with benzamidine, diisopropyl phosphofluoridate and p-nitrophenyl-p′-guanidinobenzoate indicate that the activating enzyme is a trypsin-like serine protease. An endogenous protease inhibitor, isolated from the hemolymph of Manduca larvae, inhibits the prophenoloxidase activation mediated by this enzyme. These results indicate that the probable physiological role of endogenous protease inhibitor is to control the undesired activation of prophenoloxidase in the hemolymph.

【 授权许可】

Unknown