| Range |
0.4×10^6 - 0.6×10^6 M^-1×sec^-1
|
| Organism |
Unspecified |
| Reference |
Northrup SH, Erickson HP. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci U S A. 1992 Apr 15 89(8):3338-42. p.3338 left column bottom paragraphPubMed ID1565624
|
| Primary Source |
[2] Kellett, G. L. & Gutfreund, H. (1970) Reactions of haemoglobin dimers after ligand dissociation. Nature (London) 227, 921-926. [3] Ip, S. H. C., Johnson, M. L. & Ackers, G. K. (1976) Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates. Biochemistry 15, 654-660.PubMed ID5448994, 1252417
|
| Method |
Primary source [3] abstract: "Combination of the dissociation rate constants determined by haptoglobin binding with stopped-flow determinations of the rate constant for reassociation of dissociated dimers provides an estimate of the equilibrium constant, 0K2, for the deoxyhemoglobin dimer-tetramer equilibrium." |
| Comments |
p.3338 left column bottom paragraph: "The association of hemoglobin dimers to form tetramers has k2 = 0.4-0.6×10^6 M^-1×s^-1 (primary sources)." |
| Entered by |
Uri M |
| ID |
112537 |