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Figure 1 | BMC Biochemistry

Figure 1

From: The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases

Figure 1

Leucyl aminopeptidase behaves as an approximately 200-kDa homo-oligomer under electrophoresis and lacks interchain disulfide bonds. (A), gel zymographic experiments of total proteins of T. cruzi show a leucyl aminopeptidolytic activity upon Leu-AMC under UV light (lane 1). The same gel was Coomassie-stained (lane 2). Two purification steps of native LAPTc: DEAE-Sepharose column fraction (lane 3), Superose-6 column fraction without (lane 4) or with (lane 5) previous boiling, and under reducing (lanes 4 and 5) or nonreducing (lanes 6 and 7) conditions. (B), western blot analysis of LAPTc after 8% SDS-PAGE of epimastigote total proteins with (lanes 1 and 3) or without (lane 2) previous boiling, showing both oligomeric (arrow) and monomeric (arrowhead) forms of the enzyme. (C), purified rLAPTc was subjected to 8% SDS-PAGE zymography without previous boiling of the sample (lane 1). The same gel was subsequently stained with Coomassie Blue (lane 2). The recombinant enzyme was also subjected to PAGE in the presence of 0.1 (lane 3) or 0.01% SDS (lane 4). Arrow and arrowhead indicate oligomeric and monomeric forms of the enzyme, respectively.

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BMC Biochemistry

ISSN: 1471-2091

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