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. 2019 Jan 14;151(5):670–679. doi: 10.1085/jgp.201812214

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© 2019 Gregorich et al.

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Figure 4. — Top-down proteomic analysis of contractile protein phosphorylation in ENH^+/+ and ENH^−/− mouse myocardium. (A–D) Representative zoomed-in deconvoluted mass spectra showing the relative intensities of unmodified and modified forms of cTnT isoforms (A), cTnI (B), αTpm (C), and RLC_v (D) in ENH^+/+ and ENH^−/− mouse myocardium. Reported masses are the most abundant masses. Squares, stars, and diamonds denote peaks corresponding to proteins associated noncovalently with phosphoric acid (+H₃PO₄), proteins associated noncovalently with sodium ions (+Na⁺), and proteins displaying a 62-Da mass increase relative to the unmodified and modified protein species, respectively.