Table 1.

A comparison of cleavage efficiencies

Agent	Vmax, nM sec−1	Turnover,* sec−1	Comparison to EDTA†
Enzymatic
BamHI	0.024  ± 0.001	0.007‡	4.8  × 105
Small molecule catalyzed
Esperamicin A1	0.007  ± 0.001§	0.009	6.1  × 105
Calicheamicin γ′1	0.011  ± 0.002§	0.007	4.8  × 105
Bleomycin	0.009  ± 0.001§	0.001	6.8  × 104
Methidiumpropyl-EDTA	0.003  ± 0.001§	2.4  × 10−5	1.6  × 103
Methidiumpropyl-EDTA	0.118  ± 0.004¶	0.002	1.6  × 103
EDTA	0.002  ± 0.001¶	1.5  × 10−6	1.0

^*Defined as V_max/[Agent]. 

^† Fold enhancement over EDTA turnover. 

^‡ Also known as k_cat. 

^§ [DNA]_total = 3.2 nM. 

^¶ [DNA]_total = 32 nM.