TY - JOUR
T1 - Manganese hemoglobin
T2 - Allosteric effects in stopped flow flash photolysis and sedimentation measurements
AU - Gibson, Q. H.
AU - Hoffman, B. M.
AU - Crepeau, R. H.
AU - Edelstein, S. J.
AU - Bull, C.
N1 - Funding Information:
Acknowledgments: We are indebted to Anne Griffin for technical assistance. C.B. is a predoctoral trainee of the USPHS, administered by the National Institutes Institutes of Health, training grant GM00626. This work was supported by the National Institutes of Health, Grants HL-135~I (BMH), GM-14276-08 (QHG)~ and HL-13591 (SJE) and by the National Science Foundation~ Grant GB8773 (SJE).
PY - 1974/7/10
Y1 - 1974/7/10
N2 - Conformational differences between manganese hemoglobin and its liganded derivatives are observed in the tetramer-dimer dissociation equilibrium, in the binding of 8-hydroxy-1,3,6-pyrenetrisulfonate (an analogue of 2,3-diphosphoglycerate) and bromthymol blue, and in the reaction with p-hydroxymercuribenzoate. The reaction of manganese hemoglobin with NO is readily followed by stopped flow, the resulting NO derivative is photodissociable, and rapid kinetic measurements exhibit the hemoglobin allosteric interaction.
AB - Conformational differences between manganese hemoglobin and its liganded derivatives are observed in the tetramer-dimer dissociation equilibrium, in the binding of 8-hydroxy-1,3,6-pyrenetrisulfonate (an analogue of 2,3-diphosphoglycerate) and bromthymol blue, and in the reaction with p-hydroxymercuribenzoate. The reaction of manganese hemoglobin with NO is readily followed by stopped flow, the resulting NO derivative is photodissociable, and rapid kinetic measurements exhibit the hemoglobin allosteric interaction.
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U2 - 10.1016/S0006-291X(74)80186-5
DO - 10.1016/S0006-291X(74)80186-5
M3 - Article
C2 - 4842296
AN - SCOPUS:0016219732
VL - 59
SP - 146
EP - 151
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -