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Chymotrypsin inhibitors in mosquitoes: Activity profile during development and after blood feeding
Author(s) -
Hörler Emanuel,
Briegel Hans
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1997)36:4<315::aid-arch5>3.0.co;2-q
Subject(s) - chymotrypsin , biology , blood meal , aedes aegypti , trypsin , subtilisin , biochemistry , proteases , serine proteinase inhibitors , pancreatic elastase , enzyme , elastase , serine protease , protease , larva , food science , ecology
Chymotrypsin and trypsin inhibitors persist throughout all developmental instars of Aedes aegypti . After a blood meal, inhibitor activity against chymotrypsin was more than double that of sugar‐fed females, but only weak activity was detected in midguts where proteinase inhibitors has been thought to regulate proteinases during blood digestion. A fourfold increase in the ratio of abdominal/thoracic inhibitor activity after the blood meal strongly suggested that fat body, or other abdominal tissues, represent the major source of inhibitor. Chymotrypsin inhibitor activity was deposited in maturing oocytes. Similar results were obtained with blood‐fed Anopheles albimanus . Chymotrypsin inhibitor was active against different mosquito proteinases and against bovine α‐chymotrypsin and trypsin, but not against subtilisin, pancreatic elastase, or fungal proteases; chymotrypsin inhibitors did not interfere with bacterial growth. The hypothesis on the regulation of blood digestion through the action of proteinase inhibitors during the gonotrophic cycle was abandoned and its involvement in the phenoloxidase cascade in the mosquito egg chorion is suggested instead. Arch. Insect Biochem. Physiol. 36:315–333, 1997. © 1997 Wiley‐Liss, Inc.