Thus, in the presence of the inhibitor, the enzyme's effective "K"m and "V"max become (α/α')"K"m and (1/α')"V"max, respectively. However, the modified Michaelis-Menten equation assumes that binding of the inhibitor to the enzyme has reached equilibrium, which may be a very slow process for inhibitors with sub-nanomolar dissociation constants. In these cases, it is usually more practical to treat the tight-binding inhibitor as an irreversible inhibitor (see below); however, it can still be possible to estimate "K"i' kinetically if "K"i is measured independently.