Fig. 1. (A) Buffer-corrected tryptophan fluorescence spectra of Gillichthys mirabilis and G. seta muscle-type lactate dehydrogenases (A₄-LDHs) at 20 °C. Excitation wavelength was 295 nm. (B) Thermal denaturation profiles of the A₄-LDH forms monitored using tryptophan fluorescence (excitation wavelength 295 nm, emission wavelength 377 nm). Curves were fitted to the data as described in the text. Gillichthys mirabilis A₄-LDH T_m=58.4±0.1 °C and G. seta A₄-LDH T_m=55.5±0.1 °C.

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