| Autor: |
Ochanda, James O., Oduor, Eva A. C., Galun, Rachel, Imbuga, Mabel O., Mumcuoglu, Kosta Y. |
| Předmět: |
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| Zdroj: |
Physiological Entomology; Sep2000, Vol. 25 Issue 3, p242-246, 5p, 2 Black and White Photographs, 4 Graphs |
| Abstrakt: |
SummaryThe 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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