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dc.contributor.authorOchanda, James O
dc.contributor.authorOduor, Eva A. C
dc.contributor.authorGalun, Rachel
dc.contributor.authorImbuga, Mabel O
dc.contributor.authorMumcuoglu, Kosta Y
dc.date.accessioned2013-06-19T15:29:35Z
dc.date.available2013-06-19T15:29:35Z
dc.date.issued1998
dc.identifier.citationJames O. Ochanda, Eva A. C. Oduor, Rachel Galun, Mabel O. Imbuga, Kosta Y. Mumcuoglu (1998). Partial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanus. Physiological Entomology Volume 23, Issue 4, pages 382–387, September 1998en
dc.identifier.urihttp://onlinelibrary.wiley.com/doi/10.1046/j.1365-3032.1998.234096.x/abstract
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/36425
dc.description.abstractA 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.en
dc.language.isoenen
dc.titlePartial characterization and post‐feeding activity of midgut aminopeptidase in the human body louse, Pediculus humanus humanusen
dc.typeArticleen


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