Partial purification of the aminopeptidase from the midgut of the human body louse, Pediculus humanus humanus
Date
2000Author
Ochanda, J O
Oduor, E A C
Galun, R
Imbuga, M O
Mumcuoglu, K Y
Type
ArticleLanguage
enMetadata
Show full item recordAbstract
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.
URI
http://onlinelibrary.wiley.com/doi/10.1046/j.1365-3032.2000.00186.x/abstract?deniedAccessCustomisedMessage=&userIsAuthenticated=falsehttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/48076
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.xPublisher
University of Nairobi Department of Biochemistry