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Partial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus
Author(s) -
Ochanda James O.,
Oduor Eva A. C.,
Galun Rachel,
Imbuga Mabel O.,
Mumcuoglu Kosta Y.
Publication year - 1998
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1046/j.1365-3032.1998.234096.x
Subject(s) - midgut , aminopeptidase , biology , enzyme , enzyme assay , biochemistry , leucine , larva , amino acid , ecology
Abstract. A leucine aminopeptidase was found in the midgut of the human body louse, Pediculus humanus humanus L. (Anoplura: Pediculidae). The enzyme is activated by the bloodmeal with a pH optimum at 8. The enzyme is soluble in both aqueous and detergent‐containing solutions. The two forms of the enzyme had the same Km but exhibited different catalytic activities with regard to Vmax values in these solutions. The enzyme is inhibited competitively by a substrate analogue 1,10‐phenanthroline and by Mn 2+ ions in the presence and absence of detergent.