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. 2000 Feb 9;20(8):963–970. doi: 10.1016/S0196-9781(99)00089-3

Table 2.

Comparison of the kinetic constants calculated for the noninhibited reaction and the inhibited reaction

Kinetic constants Noninhibited reactiona Inhibited reactionb
Vmax nmol/min/50 ng 130 ± 9 80 ± 5
Km mM 0.8 ± 0.1 0.3 ± 0.07
a

The Met-enk and aminopeptidase M reaction.

b

The Met-enk and aminopeptidase M reaction in the presence of Ac-Met-enk.

P < 0.01.