. Author manuscript; available in PMC: 2011 May 1.

Published in final edited form as: J Mol Cell Cardiol. 2010 Jan 15;48(5):934–942. doi: 10.1016/j.yjmcc.2010.01.005

Table II.

Summary of kinetic constants for phosphorylation of cTnT-Thr²⁰³ and cTnT-Thr²⁸⁴ by PKC-α.

Sample	Phosphorylated	K_m(app)	V_max	V_max/K_m(app)
	Residue	(µM)	(units•µL⁻¹)	(units•µL⁻¹•µM⁻¹)
cTnT-wt	T²⁰³	4.85 ± 0.83	1.62 ± 0.18	0.33 ± 0.08
cTnT-ΔK210	T²⁰³	5.09 ± 0.97	1.31 ± 0.12	0.26 ± 0.05

cTn-wt	T²⁰³	3.74 ± 0.67	0.615 ± 0.05	0.16 ± 0.03
cTn-ΔK210	T²⁰³	2.49 ± 0.29	1.22 ± 0.06	0.49 ± 0.06

cTnT-wt	T²⁸⁴	4.43 ± 0.96	1.59 ± 0.18	0.36 ± 0.09
cTnT-ΔK210	T²⁸⁴	7.40 ± 0.93	1.66 ± 0.29	0.22 ± 0.07

cTn-wt	T²⁸⁴	9.24 ± 0.75	1.76 ± 0.13	0.19 ± 0.02
cTn-ΔK210	T²⁸⁴	8.04 ± 0.88	1.90 ± 0.26	0.24 ± 0.06

In vitro kinase assays (Fig 6) were used to estimate the apparent Michaelis-Menten constant K_m(app), V_max (the maximum rate of reaction at infinite substrate concentration) and the ratio V_max/K_m(app) which denotes catalytic efficiency. Values are means ± SEM.