dc.contributor.author | Ochanda, J O | |
dc.contributor.author | Oduor, E A C | |
dc.contributor.author | Galun, R | |
dc.contributor.author | Imbuga, M O | |
dc.contributor.author | Mumcuoglu, K Y | |
dc.date.accessioned | 2013-07-16T09:42:47Z | |
dc.date.available | 2013-07-16T09:42:47Z | |
dc.date.issued | 2000 | |
dc.identifier.citation | Ochanda, J. O., Oduor, E. A. C., Galun, R., Imbuga, M. O. and Mumcuoglu, K. Y. (2000), Partial purification of the aminopeptidase from the midgut of the human body louse, Pediculus humanus humanus. Physiological Entomology, 25: 242–246. doi: 10.1046/j.1365-3032.2000.00186.x | en |
dc.identifier.uri | http://onlinelibrary.wiley.com/doi/10.1046/j.1365-3032.2000.00186.x/abstract?deniedAccessCustomisedMessage=&userIsAuthenticated=false | |
dc.identifier.uri | http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/48076 | |
dc.description.abstract | The midgut of the human body louse Pediculus humanus humanus contains a thermally stable leucine aminopeptidase, which was detected by agarose gel electrophoresis using l-amino oxidase. Midgut extracts were homogenized in saline or in 1% Triton X-100 and the aminopeptidase was purified by Superose 6 gel filtration chromatography. A peak with enzyme activity that was extracted with or without Triton X-100 was eluted at a molecular weight 67–69 kDa. Non-denaturing polyacrylamide gel electrophoresis resolved one band of molecular weight of 69 kDa for samples that were extracted in a saline buffer. Two closely linked bands of molecular weight 67 kDa and 69 kDa were observed in samples that were extracted in 1% Triton X-100. | en |
dc.language.iso | en | en |
dc.publisher | University of Nairobi | en |
dc.subject | Aminopeptidase;digestive enzyme;human body louse;Pediculus humanus humanus | en |
dc.title | Partial purification of the aminopeptidase from the midgut of the human body louse, Pediculus humanus humanus | en |
dc.type | Article | en |
local.publisher | Department of Biochemistry | en |