. Author manuscript; available in PMC: 2014 Aug 1.

Published in final edited form as: Biochim Biophys Acta. 2013 Apr 10;1830(8):4218–4228. doi: 10.1016/j.bbagen.2013.04.005

Table 1.

IC₅₀ of inhibition of amidolytic (L-BAPNA and Ac-Lys-pNA), aminopeptidase (H-Arg-AMC) and proteolytic activities of gingipains by PDs

Enzyme	Substrate	PD_RgpB	PD_HRgpA	PD_Kgp
RgpB	L-BAPNA	23.7 nM	15.7 nM	n.i.
	H-Arg-AMC	7.2 nM	6.9 nM	n.i.
	Azocoll	7.1 nM	7.3 nM	n.i.
HrgpA	L-BAPNA	12.6 nM	9.6 nM	n.i.
	H-Arg-AMC	4.9 nM	4.5 nM	n.i.
	Azocoll	5.8 nM	5.3 nM	n.i.
Kgp^(a)	Ac-Lys-pNA	>100 µM	>100 µM	n.i.
Kgp^(a)	Azocoll	7.9 µM	13.9 µM	n.i.

n.i. – no inhibition

IC₅₀ is an average calculated from two independent experiments.

^(a)

PDs in the final concentration range from 1 µM to 200 µM were used to determine IC₅₀ of Kgp inhibition.