Monod—Wyman—Changeux and derived parameters for intact orbiniid hemoglobin molecules at pH 6.77 and 7.60
| pH . | P50 . | Pm . | n50 . | nmax . | KT . | KR . | L . | Q . | ▵G . |
|---|---|---|---|---|---|---|---|---|---|
| 6.77 | 1.23 | 1.17 | 1.86 | 1.88 | 0.348±0.0152 | 3.682±0.573 | 570 | 4.34 | 5.29 |
| 7.60 | 0.58 | 0.59 | 1.86 | 1.86 | 0.366±0.0713 | 6.958±1.041 | 87 | 3.19 | 6.42 |
| pH . | P50 . | Pm . | n50 . | nmax . | KT . | KR . | L . | Q . | ▵G . |
|---|---|---|---|---|---|---|---|---|---|
| 6.77 | 1.23 | 1.17 | 1.86 | 1.88 | 0.348±0.0152 | 3.682±0.573 | 570 | 4.34 | 5.29 |
| 7.60 | 0.58 | 0.59 | 1.86 | 1.86 | 0.366±0.0713 | 6.958±1.041 | 87 | 3.19 | 6.42 |
See Weber et al. (1995) for details of the curve-fitting and calculations.
KT, oxygen association constant of the low-affinity state (T,tense); KR, oxygen association constant of the high-affinity state(R, relaxed) (values are S.E. of the fitted parameters as estimated in the fitting procedure, the Levenberg—Morquordt method); L,allosteric constant; n50, Hill's cooperativity coefficient; nmax, maximum cooperativity; P50, oxygen pressure at half-saturation; Pm, median oxygen pressure; Q, number of interacting oxygen-binding sites; ▵G, free energy of heme—heme interaction.