Báo cáo Y học: The a1b1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen Further evidence from the iron valency hybrids
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When theaand bchains were separated from humanoxyhemoglobin (HbO2), each individual chain was oxidizedeasily to the ferric form, their rates being almost the samewith a very strong acid-catalysis. In the HbO2tetramer, ontheother hand, bothchains become considerably resistant toautoxidation over a wide range of pH values (pH 5±11).
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Báo cáo Y học: The a1b1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen Further evidence from the iron valency hybrids
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Báo cáo Y học: The a1b1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen Further evidence from the iron valency hybrids
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