Table 2. Summary of calculated Michaelis-Menten kinetic parameters from the data presented in Fig 8.

Peptide Name	Peptide Sequence	km (μM)	95% CI	Vmax (μM s-1)	95% CI
No added salt
Hs H2B (23–37)	Ac-KKDGKKRKRSRKESY-amide	0.6	[0.3, 1.0]	17000	[15000, 19000]
Mono R	Ac-KKGGRGGGGKKY-amide	1.4	[0.9, 2.3]	990	[870, 1100]
RGR	Ac-KKGGRGRGGKKY-amide	0.7	[0.4, 1.2]	2400	[2200, 2700]
KRGR	Ac-KKGKRGRGGKKY-amide	0.6	[0.3, 1.0]	1200	[950, 1400]
RKR	Ac-KKGGRKRGGKKY-amide	0.6	[0.3, 0.9]	1700	[1500, 2000]
RGRK	Ac-KKGGRGRKGKKY-amide	0.5	[0.3, 0.8]	970	[840, 1100]
RER	Ac-KKGGRERGGKKY-amide	2.8	[1.7, 4.6]	750	[640, 880]
+130 mM KCl
Hs H2B (23–37)	Ac-KKDGKKRKRSRKESY-amide	17	[14, 20]	16000	[15000, 17000]
Mono R	Ac-KKGGRGGGGKKY-amide	—*	—*	—*	—*
RGR	Ac-KKGGRGRGGKKY-amide	6.2	[3.5, 11]	820	[690, 980]
KRGR	Ac-KKGKRGRGGKKY-amide	3.3	[1.7, 7.0]	550	[440, 700]
RKR	Ac-KKGGRKRGGKKY-amide	6.9	[3.8, 16]	880	[710, 1200]
RGRK	Ac-KKGGRGRKGKKY-amide	2.4	[1.3, 4.5]	400	[330, 490]
RER	Ac-KKGGRERGGKKY-amide	—*	—*	—*	—*

All kinetic values and their 95% confidence intervals were obtained using the “statistical analysis” function in GraphPad Prism version 8.0.1.

*indicates poor fit of Michaelis-Menten equation