Rapid Elimination of Blood Alcohol Using Erythrocytes: Mathematical Modeling and In Vitro Study

Table 1

Kinetic constants for ADH, ALD, and LDH.

Constant	ADH	ALD	LDH
Ka, µM	180 (K11)	20 (K21)	24 (K31)
Kb, µM	17000 (K12)	9 (K22)	120 (K32)
Kp, µM	800 (K13)		6000 (K33)
Kq, µM	100 (K14)		100 (K34)
Kia, µM	270 (K15)	70 (K25)	8 (K35)
Kib, µM	90000 (K16)		130 (K36)
Kip, µM	1100 (K17)		130000 (K37)
Kiq, µM	31 (K18)	100 (K28)	100 (K38)
Vf(Et), s^−1	40 (V11)	1 (V21)	550 (V31)
Vr(Et), s^−1	340 (V12)		60 (V32)
,	22		3.8

, K_b, K_p, and K_q are Michaelis constants. K_i is the constant of inhibition. is the equilibrium constant.
The indexes a, b, p, and q denote the following substrates (in the order of their association with and dissociation from the corresponding enzyme): NAD⁺, ethanol, acetaldehyde, and NADH (for ADH [15, 16]); NAD⁺, acetaldehyde, acetate, and NADH (for ALD [17–20]); and NADH, pyruvate, lactate, and NAD⁺ (for LDH [21, 22]), respectively.