. Author manuscript; available in PMC: 2016 Sep 1.

Published in final edited form as: Anal Biochem. 2015 Jun 4;484:148–153. doi: 10.1016/j.ab.2015.05.020

Table 1.

Properties of luciferases^a

Enzyme	Relative Specific Activity^b		K_m (μM)		Bioluminescence λ_max^c (nm)		Thermal Inactivation^d (h) at 37°C

	Flash Height	Integrated	LH2	Mg-ATP	pH 7.8	pH 6.5
PpyWT	100 ± 4	100 ± 2	15 ± 2	86 ± 7	560 (70)	609, 560 sh (92)	0.3 ± 0.03
PpyLit	180 ± 10	200 ± 12	25 ± 2	53 ± 6	560 (69)	561, 610 sh (90)	0.07 ± 0.02
PLG2	135 ± 5	425 ± 2	52 ± 6	79 ± 5	559 (67)	561 (71)	> 24 ± 5

The data for PpyWT and PpyLit and the methods used to produce the values for PLG2 are described in reference [37].

Specific activities were obtained at pH 7.8 with LH₂ (400 μM) and Mg-ATP (2 mM) and are expressed relative to PpyWT values, which are defined as 100. Integrated activities are based on total light emission in 15 min.

Bioluminescence emission maxima were obtained from two trials and the standard deviation is ± 1 nm. The bandwidth at half-maximal intensity is shown in parentheses and sh indicates a shoulder.

Time for the maximum initial activity to decay to 50% at 37 °C. All activity values were obtained from at least three trials and are reported as means ± standard deviation.