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. Author manuscript; available in PMC: 2021 Apr 1.
Published in final edited form as: Mol Microbiol. 2020 Jan 6;113(4):807–825. doi: 10.1111/mmi.14445

Figure 10. Biochemical analysis of purified AfAas1 and AfAas2.

Figure 10.

A. A Coomassie-stained SDS gel electrophoresis illustrating the purity of AfAas1 and AfAas2 used in the biochemical assays to determine the acyl acceptor (ACP or CoA) and acyl donor (12:0 or 18:1) specificities of the two enzymes.

B. Biochemical activity of AfAas1. AfAas1 activity using [14C]12:0 as substrate was linear with protein and had a specific activity of 0.38 ± 0.002 pmol/min/μg protein (Inset).

C. Biochemical activity of AfAas2. AfAas2 activity using [14C]18:1 as substrate was linear with protein and had a specific activity of 1.59 ± 0.02 pmol/min/μg protein (Inset). AfAas2 activity using [14C]12:0 as substrate was 0.57 ± 0.03 pmol/min/μg protein.