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- W1981833712 abstract "Nuclear magnetic resonance spectroscopy (100-MHz proton) was used to study the low-spin ( S = 1/2) azide derivatives of human adult (α 2 β 2 ), human fetal (α 2 γ 2 ), Zürich (α 2 β 2 63 His → Arg ), and horse (α 2 ′β 2 ′) methemoglobins, as well as whale metmyoglobin in 0.1 M deuterated phosphate at pD 7 and at 31°C. The experimental results indicate that the azide-bound heme groups of the α- and β-chains in human adult methemoglobin and of the α- and γ-chains in fetal methemoglobin are not equivalent. The affinity of the β- or γ-chain for azide ion appears larger than that of the α-chain. The nuclar magnetic resonance spectrum of hemoglobin Zürich shows that the environment of the azide-heme complex in the abnormal β-chain is altered by the substitution of arginine for histidine in the β-63 position, while the α-heme environment remains unaffected." @default.
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- W1981833712 date "1969-08-01" @default.
- W1981833712 modified "2023-09-25" @default.
- W1981833712 title "NUCLEAR MAGNETIC RESONANCE STUDIES OF HEMOGLOBINS, III. EVIDENCE FOR THE NONEQUIVALENCE OF α- AND β-CHAINS IN AZIDE DERIVATIVES OF METHEMOGLOBINS" @default.
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- W1981833712 doi "https://doi.org/10.1073/pnas.63.4.1403" @default.
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