Partial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus

Citation:
Ochanda JO, Oduor EAC, Galun R, Imbuga MO, Mumcuoglu KY. "Partial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus.". 1998.

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 Mn2+ ions in the presence and absence of detergent.

Partial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus

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