Article
Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.
The Journal of biological chemistry - 18 Mar 1994
Joshi A A, McDonald M J
Abstract excerpt
Human oxyhemoglobin assembly was evaluated in the Soret region by rapidly mixing normal and carboxypeptidase-digested chains (1-10 x 10(-6) M, heme basis) in 0.1 M Tris-HCl, 0.1 M NaCl, 1 mM EDTA, pH 7.4, at 21.5 degrees C. Rate constants of 1.14 (+/- 0.09) and 2.11 (+/- 0.06) x 10(5) M-1 S-1 were measured for the association of Des(Arg-141) alpha with beta A and alpha A with beta A chains, respectively. The...
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