Table 1. Kinetic properties of... | American Society of Hematology

Table 1.

Kinetic properties of recombinant TPIs

Enzymes	Specific activity, U/mg	k_cat/K_m, min/μM	TPI bound to MT,^*U			Activity, %
			TPI added 1.8 U		18 U	MT added
			−PEG	+PEG	−PEG	0.6 mg	3 mg
wTPI	8000	18.6	0.10	0.23	0.28	87	70
mTPI	2400	6.3	0.10	0.27	0.29	59	66

Enzymes	Specific activity, U/mg	k_cat/K_m, min/μM	TPI bound to MT,^*U			Activity, %
			TPI added 1.8 U		18 U	MT added
			−PEG	+PEG	−PEG	0.6 mg	3 mg
wTPI	8000	18.6	0.10	0.23	0.28	87	70
mTPI	2400	6.3	0.10	0.27	0.29	59	66

Different amounts of recombinant TPIs were incubated with MT (2 mg/mL) in 300 μL of 100 mM MES buffer, pH 7.0, containing 5 mM MgCl₂ and 20 μM paclitaxel, in the presence or absence of PEG (10%), at 37°C for 15 minutes. The samples were centrifuged (50 000 g, 30 minutes, 37°C), and the bound and free TPI was assayed enzymatically as described in “Materials and methods.”

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