The mosquito Aedes aegypti (L.): evidence for three new proteinases.
The effect of inhibitors was studied on the proteolytic activity of crude extracts of the mosquito Aedes aegypti (L.), prepared 25 h after blood intake. This activity is only partially inhibited by the lima bean trypsin inhibitor (LBTI) or by EDTA. Experiments with mixed inhibitors are used to indicate that, apart from the well characterized trypsin-like enzymes, at least three other proteinases are present. These are an LBTI-resistant serine proteinase, a metal chelator-sensitive proteinase, and a proteinase which can only be inhibited by the ovomucoid inhibitor. These newly described proteinases are inactive against several model substrates developed for mammalian enzymes. They are partially separable by ion-exchange chromatography.
D000330:Aedes / Q000201:enzymology*; D000818:Animals; D002364:Caseins / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D008297:Male; D003012:Microbial Collagenase / Q000378:metabolism; D010059:Ovomucin / Q000494:pharmacology; D010196:Pancreatic Elastase / Q000378:metabolism; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D011480:Protease Inhibitors; D013820:Thermolysin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000494:pharmacology
D002364:Caseins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D010059:Ovomucin; D010664:Phenylmethylsulfonyl Fluoride; D004492:Edetic Acid; D010450:Endopeptidases; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D013820:Thermolysin; D003012:Microbial Collagenase