<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ochanda, James O.</style></author><author><style face="normal" font="default" size="100%">Oduor, Eva A. C.</style></author><author><style face="normal" font="default" size="100%">Galun, Rachel</style></author><author><style face="normal" font="default" size="100%">Imbuga, Mabel O.</style></author><author><style face="normal" font="default" size="100%">Mumcuoglu, Kosta Y.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Partial characterization and post-feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus</style></title><secondary-title><style face="normal" font="default" size="100%">Physiological Entomology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">human; body louse; midgut; enzyme; leucine; aminopeptidase; Pediculus humanus; Glossina; blood; digestion; diptera; protein; insects; pediculosis; pdf</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.phthiraptera.org/Publications/38770.pdf</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">23</style></volume><pages><style face="normal" font="default" size="100%">382-387</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">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.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><accession-num><style face="normal" font="default" size="100%">38770</style></accession-num><notes><style face="normal" font="default" size="100%">Journal</style></notes></record></records></xml>