TY - JOUR
T1 - The properties and interactions of the isolated α- and β-chains of human haemoglobin
T2 - V. The reaction of α- and β-chains
AU - Antonini, Eraldo
AU - Bucci, Enrico
AU - Fronticelli, Clara
AU - Chiancone, Emilia
AU - Wyman, Jeffries
AU - Rossi-Fanelli, Alessandro
PY - 1966
Y1 - 1966
N2 - The mixing of the isolated α- and β-chains of human haemoglobin is accompanied by spectroscopic changes in the Soret region and by changes in the kinetics of the reaction with ligands and in sedimentation behaviour. These changes show that when the chains are combined with p-mercuribenzoate, the system is in a state of labile association—dissociation equilibrium which is strongly dependent on pH between pH 7 and 8, and is oxygen linked. The kinetics of the spectroscopic changes reveal that, both in the presence and absence of p-mercuribenzoate in the chains, the recombination is a complex process with an over-all half-time of the order of one to five seconds at 30°C, when the chains are at micromolar concentration.
AB - The mixing of the isolated α- and β-chains of human haemoglobin is accompanied by spectroscopic changes in the Soret region and by changes in the kinetics of the reaction with ligands and in sedimentation behaviour. These changes show that when the chains are combined with p-mercuribenzoate, the system is in a state of labile association—dissociation equilibrium which is strongly dependent on pH between pH 7 and 8, and is oxygen linked. The kinetics of the spectroscopic changes reveal that, both in the presence and absence of p-mercuribenzoate in the chains, the recombination is a complex process with an over-all half-time of the order of one to five seconds at 30°C, when the chains are at micromolar concentration.
KW - PMB
KW - p-mercuribenzoate
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U2 - 10.1016/S0022-2836(66)80092-X
DO - 10.1016/S0022-2836(66)80092-X
M3 - Article
C2 - 5961150
AN - SCOPUS:0013903325
SN - 0022-2836
VL - 17
SP - 29
EP - 46
JO - Journal of molecular biology
JF - Journal of molecular biology
IS - 1
ER -