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. 2019 Oct 14;116(44):22229–22236. doi: 10.1073/pnas.1904485116

Fig. 5.

Fig. 5.

The swst mutation causes reduced FAH protein in the liver but does not alter enzymatic activity. (A) Representative spectrometric FAH assay results with liver lysates from homozygous mutant (s/s, n = 5), heterozygous mutant (s/+, n = 5), and WT littermates (+/+, n = 4). (B) Relative enzymatic activity quantified from FAH assays in A. (C) Representative FAH assay results using purified WT and mutant FAH proteins. (D) Relative enzymatic activity quantified from FAH assays in C. Two separate experiments were performed with 2 replicates each (n = 4/group). (E) Representative immunoblots of FAH in liver lysates and relative FAH levels quantified from immunoblotting (n = 3 samples/group, average of 3 separate assays). (F) Plasma concentrations of methionine (Met), phenylalanine (Phe), and tyrosine (Tyr) in s/s (n = 5), s/+ (n = 4), and +/+ (n = 4) mice. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.