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Partial purification of the aminopeptidase from the midgut of the human body louse, Pediculus humanus humanus
Author(s) -
Ochanda James O.,
Oduor Eva A. C.,
Galun Rachel,
Imbuga Mabel O.,
Mumcuoglu Kosta Y.
Publication year - 2000
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1046/j.1365-3032.2000.00186.x
Subject(s) - midgut , biology , aminopeptidase , size exclusion chromatography , molecular mass , agarose gel electrophoresis , agarose , microbiology and biotechnology , electrophoresis , chromatography , polyacrylamide gel electrophoresis , biochemistry , enzyme , leucine , larva , amino acid , chemistry , gene , botany
Summary 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.