@article {108,
	title = {Partial characterization and post-feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus},
	journal = {Physiological Entomology},
	volume = {23},
	year = {1998},
	month = {1998},
	pages = {382 - 387},
	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.},
	keywords = {aminopeptidase, blood, body louse, digestion, Diptera, enzyme, Glossina, human, Insects, leucine, midgut, pdf, pediculosis, Pediculus humanus, protein},
	url = {http://www.phthiraptera.info/Publications/38770.pdf},
	author = {Ochanda,James O. and Oduor,Eva A. C. and Galun,Rachel and Imbuga,Mabel O. and Mumcuoglu,Kosta Y.}
}
@article {116,
	title = {Characterization of body louse midgut proteins recognized by resistant hosts},
	journal = {Medical and Veterinary Entomology},
	volume = {10},
	year = {1996},
	month = {1996},
	pages = {35 - 38},
	abstract = {The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS- PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kda and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F- 1, F-2, F-3, and F-4) when resolved on a 18\% SDS-PAGE. The F-1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.},
	keywords = {adult, antigens, arthropod, body, Boophilus, cattle, control, human, immunization, immunogens, immunological, louse, midgut, pdf, Pediculus humanus, protein, ticks, vaccinated, vaccine},
	url = {http://www.phthiraptera.info/Publications/38618.pdf},
	author = {Ochanda,James O. and Mumcuoglu,Kosta Y. and Ben-Yakir,David and Okuru,J. K. and Oduol,V. O. and Galun,Rachel}
}
