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. 2006 Aug 2;61(5):1187–1195. doi: 10.1111/j.1365-2958.2006.05307.x

Figure 3.

Figure 3

Identification of PfUCH54 by mass spectrometry. P. falciparum and uninfected erythrocyte lysates were reacted with HA‐Ub‐VME probe on a preparative scale followed by SDS‐PAGE. Parasite‐specific reactive proteins were extracted and subjected to tandem mass spectrometry. Identified polypeptides (indicated in pink) were screened against the P. falciparum genome database and matched a 465‐amino‐acid protein annotated as a putative C‐terminal Ub hydrolase. Mass spectrometry properties of the identified peptides are shown. MH+ indicates the protonated mass of each peptide; %Mass represents the per cent of the total protein mass occupied by each peptide; AA indicates the span of amino acids covered by each peptide; and %AA identifies the per cent of amino acid coverage. Black arrows indicate potential alternative internal start sites as determined by additional translation products seen in Fig. 5.