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Bloodmeal digestion in the midgut of Phlebotomus papatasi and Phlebotomus langeroni
Author(s) -
DILLON R. J.,
LANE P.
Publication year - 1993
Publication title -
medical and veterinary entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 82
eISSN - 1365-2915
pISSN - 0269-283X
DOI - 10.1111/j.1365-2915.1993.tb00681.x
Subject(s) - midgut , biology , digestion (alchemy) , protease , trypsin , psychodidae , aminopeptidase , phlebotomus , leucyl aminopeptidase , microbiology and biotechnology , chymotrypsin , enzyme , biochemistry , leishmania , leishmaniasis , parasite hosting , botany , larva , chemistry , immunology , chromatography , amino acid , leucine , world wide web , computer science
. Bloodmeal digestion in midguts of the sandflies Phlebotomus papatasi and Phlebotomus langeroni (Diptera: Psychodidae) was investigated in optimized assays to detect general protease, trypsin and aminopeptidase activities using synthetic substrates. Optimal activity occurred at pH 8‐9 for all enzymes examined in both species. Protease activity peaked at 24‐34h post human bloodmeal in midguts of P.papatasi and 34‐48h in P'.langeroni; all endo‐ and exoprotease activities were completed by 50 h in P.papatasi compared to 72 h in P. langeroni. Hydrolysis of two chymotrypsin substrates was <2% of trypsin activity in both species. Aminopeptidase activity was associated mainly with the midgut wall, whereas trypsin activity was confined to the midgut lumen. A feature of digestion in P.langeroni was the high level of aminopeptidase recorded within 10h of the bloodmeal.