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. 2017 Mar 27;292(20):8244–8261. doi: 10.1074/jbc.M117.775031

Table 2.

Processing of wild-type and mutant proMPO

Stably transfected HEK cells expressing wild-type or mutant MPO were radiolabeled biosynthetically, and MPO-related proteins were immunoprecipitated immediately after labeling (at 0 h) and 20 h after chase. Immunoprecipitates were separated by SDS-PAGE. The amount of immunoprecipitated 90- and 59-kDa MPO-related protein at 20 h of chase and the amount of MPO-related protein secreted was quantitated using a phosphorimaging device.

Source 90 kDa:59 kDa (n)a % Secretedb
Wild-type MPO 0.72 ± 0.08 (13) 100
C319A 1.96 ± 0.27 (5) 28.8 ± 7.9
C158A 1.62 ± 0.24 (6) 5.1 ± 2.0
C158A/C319A 1.64 ± 0.30 (4) 11.9 ± 1.3

a The ratio of precursor to mature MPO (90 kDa:59 kDa) is shown as mean ± S.E. for n number of experiments. The p values for the differences of 90 kDa:59 kDa for C319A, C158A, and C158A/C319A versus that of wild-type MPO are .0001, .0003, and .0009, respectively.

b The percent MPO-related protein normalized to that secreted by HEK-MPO cells is shown as the mean ± S.E. for four separate experiments.